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Conserved domains on  [gi|568907554|ref|XP_006496493|]
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arf-GAP domain and FG repeat-containing protein 1 isoform X1 [Mus musculus]

Protein Classification

COG5347 and ArfGap_AGFG1 domain-containing protein( domain architecture ID 13429539)

protein containing domains COG5347, ArfGap_AGFG1, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArfGap_AGFG1 cd08857
ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain ...
 13-128 1.20e-89

ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG1 is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG1 plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG1 promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication.


:

Pssm-ID: 350082 [Multi-domain]  Cd Length: 116  Bit Score: 271.91  E-value: 1.20e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  13 HLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08857    1 HLKMLREMTSLPHNRKCFDCDQRGPTYANMTVGSFVCTSCSGILRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568907554  93 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 128
Cdd:cd08857   81 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 116
COG5347 super family cl34987
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 8-268 1.03e-15

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


The actual alignment was detected with superfamily member COG5347:

Pssm-ID: 227651 [Multi-domain]  Cd Length: 319  Bit Score: 78.28  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   8 KQEEKHLKMLRDMtgLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHG 85
Cdd:COG5347    4 KSEDRKLLKLLKS--DSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLG-VHisKVKSLTLDNWTEEELRRMEVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  86 NEVCKQIWLGlfDDRSSAIPDFR---DPQKVKEFLQEKYEKKRWYVPPEQAKVVASvhasisgssaSSTSSTPEVKPLKS 162
Cdd:COG5347   81 NSNANRFYEK--NLLDQLLLPIKakyDSSVAKKYIRKKYELKKFIDDSSSPSDFSS----------FSASSTRTVDSVDD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554 163 LL-GESAPALHLNKGTPSQSP--VVGRSQGQQQEKKQFDLLSDL---GSDIFAAPAPQSTATANFAN--FAHFNSHAAQN 234
Cdd:COG5347  149 RLdSESQSRSSSASLGNSNRPddELNVESFQSTGSKPRSLTSTKsnkDNLLNSELLTLNSLLSSNSEvgSGTKSRSDAQE 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568907554 235 SANADFANFDAFGQSSGSSNFGGFPTASHSSFQP 268
Cdd:COG5347  229 KSSTKATESVKPGPVNTSSTSSLPPAIKRSPVQQ 262
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 385-575 2.81e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.80  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  385 SSAATSSNAYTPTSNASSSVFGTVPVGASAQTQPASSgpAPFGATPSTNPFVAATGPSAASSTNpfqTNARGATGLSGAM 464
Cdd:pfam17823 107 ADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFS--APRAAACRANASAAPRAAIAAASAP---HAASPAPRTAASS 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  465 HSQVFPHAHFAATFGTASMSMPAGFgTPAQySLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGA-GFATFGQTKPVVTP 543
Cdd:pfam17823 182 TTAASSTTAASSAPTTAASSAPATL-TPAR-GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAvGTVTPAALATLAAA 259

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568907554  544 FGQVAAAGVSSNP----FMTGAPTGQLPTGSSSTNP 575
Cdd:pfam17823 260 AGTVASAAGTINMgdphARRLSPAKHMPSDTMARNP 295
 
Name Accession Description Interval E-value
ArfGap_AGFG1 cd08857
ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain ...
 13-128 1.20e-89

ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG1 is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG1 plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG1 promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication.


Pssm-ID: 350082 [Multi-domain]  Cd Length: 116  Bit Score: 271.91  E-value: 1.20e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  13 HLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08857    1 HLKMLREMTSLPHNRKCFDCDQRGPTYANMTVGSFVCTSCSGILRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568907554  93 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 128
Cdd:cd08857   81 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 116
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 14-135 2.28e-44

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 [Multi-domain]  Cd Length: 119  Bit Score: 153.27  E-value: 2.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554    14 LKMLRDMtglPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPpHR--VKSISMTTFTQQEIEFLQKHGNEVCKQ 91
Cdd:smart00105   1 LKLLRSI---PGNKKCFDCGAPNPTWASVNLGVFLCIECSGIHRSLGV-HIskVRSLTLDTWTEEELRLLQKGGNENANS 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568907554    92 IWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWyVPPEQAKV 135
Cdd:smart00105  77 IWESNLDDFSLKPPDDDDQQKYESFIAAKYEEKLF-VPPESAEE 119
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 15-130 6.49e-38

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: 460200 [Multi-domain]  Cd Length: 117  Bit Score: 135.81  E-value: 6.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   15 KMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGL-NPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:pfam01412   2 RVLRELLKLPGNKVCADCGAPNPTWASVNLGIFICIDCSGVHRSLgVHISKVRSLTLDTWTDEQLELMKAGGNDRANEFW 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568907554   94 LGLFDDrSSAIPDFRDPQKVKEFLQEKYEKKRWYVPP 130
Cdd:pfam01412  82 EANLPP-SYKPPPSSDREKRESFIRAKYVEKKFAKPG 117
PLN03131 PLN03131
hypothetical protein; Provisional
 7-126 1.37e-23

hypothetical protein; Provisional


Pssm-ID: 178677 [Multi-domain]  Cd Length: 705  Bit Score: 105.24  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   7 RKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNppHRVKSISMTTFTQQEIEFLQKHGN 86
Cdd:PLN03131   4 RKEEERNEKIIRGLMKLPPNRRCINCNSLGPQFVCTNFWTFICMTCSGIHREFT--HRVKSVSMSKFTSQDVEALQNGGN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568907554  87 EVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:PLN03131  82 QRAREIYLKDWDQQRQRLPDNSKVDKIREFIKDIYVDKKY 121
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 8-268 1.03e-15

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


Pssm-ID: 227651 [Multi-domain]  Cd Length: 319  Bit Score: 78.28  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   8 KQEEKHLKMLRDMtgLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHG 85
Cdd:COG5347    4 KSEDRKLLKLLKS--DSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLG-VHisKVKSLTLDNWTEEELRRMEVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  86 NEVCKQIWLGlfDDRSSAIPDFR---DPQKVKEFLQEKYEKKRWYVPPEQAKVVASvhasisgssaSSTSSTPEVKPLKS 162
Cdd:COG5347   81 NSNANRFYEK--NLLDQLLLPIKakyDSSVAKKYIRKKYELKKFIDDSSSPSDFSS----------FSASSTRTVDSVDD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554 163 LL-GESAPALHLNKGTPSQSP--VVGRSQGQQQEKKQFDLLSDL---GSDIFAAPAPQSTATANFAN--FAHFNSHAAQN 234
Cdd:COG5347  149 RLdSESQSRSSSASLGNSNRPddELNVESFQSTGSKPRSLTSTKsnkDNLLNSELLTLNSLLSSNSEvgSGTKSRSDAQE 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568907554 235 SANADFANFDAFGQSSGSSNFGGFPTASHSSFQP 268
Cdd:COG5347  229 KSSTKATESVKPGPVNTSSTSSLPPAIKRSPVQQ 262
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 385-575 2.81e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.80  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  385 SSAATSSNAYTPTSNASSSVFGTVPVGASAQTQPASSgpAPFGATPSTNPFVAATGPSAASSTNpfqTNARGATGLSGAM 464
Cdd:pfam17823 107 ADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFS--APRAAACRANASAAPRAAIAAASAP---HAASPAPRTAASS 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  465 HSQVFPHAHFAATFGTASMSMPAGFgTPAQySLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGA-GFATFGQTKPVVTP 543
Cdd:pfam17823 182 TTAASSTTAASSAPTTAASSAPATL-TPAR-GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAvGTVTPAALATLAAA 259

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568907554  544 FGQVAAAGVSSNP----FMTGAPTGQLPTGSSSTNP 575
Cdd:pfam17823 260 AGTVASAAGTINMgdphARRLSPAKHMPSDTMARNP 295
 
Name Accession Description Interval E-value
ArfGap_AGFG1 cd08857
ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain ...
 13-128 1.20e-89

ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1); The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG1 is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG1 plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG1 promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication.


Pssm-ID: 350082 [Multi-domain]  Cd Length: 116  Bit Score: 271.91  E-value: 1.20e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  13 HLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08857    1 HLKMLREMTSLPHNRKCFDCDQRGPTYANMTVGSFVCTSCSGILRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568907554  93 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 128
Cdd:cd08857   81 WLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 116
ArfGap_AGFG cd08838
ArfGAP domain of the AGFG subfamily (ArfGAP domain and FG repeat-containing proteins); The ...
 14-128 3.97e-69

ArfGAP domain of the AGFG subfamily (ArfGAP domain and FG repeat-containing proteins); The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication.


Pssm-ID: 350067 [Multi-domain]  Cd Length: 113  Bit Score: 218.60  E-value: 3.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  14 LKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNppHRVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:cd08838    1 EKILRELLKLPENKRCFDCGQRGPTYVNLTFGTFVCTTCSGIHREFN--HRVKSISMSTFTPEEVEFLQAGGNEVARKIW 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568907554  94 LGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 128
Cdd:cd08838   79 LAKWDPRTDPEPDSGDDQKIREFIRLKYVDKRWYD 113
ArfGap_AGFG2 cd17903
ArfGAP domain of AGFG2 (ArfGAP domain and FG repeat-containing protein 2); The ArfGAP domain ...
 15-128 2.60e-67

ArfGAP domain of AGFG2 (ArfGAP domain and FG repeat-containing protein 2); The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG2 is a member of the HIV-1 Rev binding protein (HRB) family and contains one Arf-GAP zinc finger domain, several Phe-Gly (FG) motifs, and four Asn-Pro-Phe (NPF) motifs. AGFG2 interacts with Eps15 homology (EH) domains and plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication.


Pssm-ID: 350090 [Multi-domain]  Cd Length: 116  Bit Score: 214.08  E-value: 2.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  15 KMLRDMTGLPH-NRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:cd17903    2 RRVRELGGCSAaNRHCFECAQRGVTYVDITVGSFVCTTCSGLLRGLNPPHRVKSISMTTFTEPEVLFLQARGNEVCRKIW 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568907554  94 LGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV 128
Cdd:cd17903   82 LGLFDARTSLIPDSRDPQKVKEFLQEKYEKKRWYV 116
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 14-135 2.28e-44

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 [Multi-domain]  Cd Length: 119  Bit Score: 153.27  E-value: 2.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554    14 LKMLRDMtglPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPpHR--VKSISMTTFTQQEIEFLQKHGNEVCKQ 91
Cdd:smart00105   1 LKLLRSI---PGNKKCFDCGAPNPTWASVNLGVFLCIECSGIHRSLGV-HIskVRSLTLDTWTEEELRLLQKGGNENANS 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568907554    92 IWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWyVPPEQAKV 135
Cdd:smart00105  77 IWESNLDDFSLKPPDDDDQQKYESFIAAKYEEKLF-VPPESAEE 119
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 15-130 6.49e-38

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: 460200 [Multi-domain]  Cd Length: 117  Bit Score: 135.81  E-value: 6.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   15 KMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGL-NPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:pfam01412   2 RVLRELLKLPGNKVCADCGAPNPTWASVNLGIFICIDCSGVHRSLgVHISKVRSLTLDTWTDEQLELMKAGGNDRANEFW 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568907554   94 LGLFDDrSSAIPDFRDPQKVKEFLQEKYEKKRWYVPP 130
Cdd:pfam01412  82 EANLPP-SYKPPPSSDREKRESFIRAKYVEKKFAKPG 117
ArfGap cd08204
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 17-121 2.96e-30

GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family of proteins containing an ArfGAP catalytic domain that induces the hydrolysis of GTP bound to the small guanine nucleotide-binding protein Arf, a member of the Ras superfamily of GTPases. Like all GTP-binding proteins, Arf proteins function as molecular switches, cycling between GTP (active-membrane bound) and GDP (inactive-cytosolic) form. Conversion to the GTP-bound form requires a guanine nucleotide exchange factor (GEF), whereas conversion to the GDP-bound form is catalyzed by a GTPase activating protein (GAP). In that sense, ArfGAPs were originally proposed to function as terminators of Arf signaling, which is mediated by regulating Arf family GTP-binding proteins. However, recent studies suggest that ArfGAPs can also function as Arf effectors, independently of their GAP enzymatic activity to transduce signals in cells. The ArfGAP domain contains a C4-type zinc finger motif and a conserved arginine that is required for activity, within a specific spacing (CX2CX16CX2CX4R). ArfGAPs, which have multiple functional domains, regulate the membrane trafficking and actin cytoskeleton remodeling via specific interactions with signaling lipids such as phosphoinositides and trafficking proteins, which consequently affect cellular events such as cell growth, migration, and cancer invasion. The ArfGAP family, which includes 31 human ArfGAP-domain containing proteins, is divided into 10 subfamilies based on domain structure and sequence similarity. The ArfGAP nomenclature is mainly based on the protein domain structure. For example, ASAP1 contains ArfGAP, SH3, ANK repeat and PH domains; ARAPs contain ArfGAP, Rho GAP, ANK repeat and PH domains; ACAPs contain ArfGAP, BAR (coiled coil), ANK repeat and PH domains; and AGAPs contain Arf GAP, GTP-binding protein-like, ANK repeat and PH domains. Furthermore, the ArfGAPs can be classified into two major types of subfamilies, according to the overall domain structure: the ArfGAP1 type includes 6 subfamilies (ArfGAP1, ArfGAP2/3, ADAP, SMAP, AGFG, and GIT), which contain the ArfGAP domain at the N-terminus of the protein; and the AZAP type includes 4 subfamilies (ASAP, ACAP, AGAP, and ARAP), which contain an ArfGAP domain between the PH and ANK repeat domains.


Pssm-ID: 350058 [Multi-domain]  Cd Length: 106  Bit Score: 114.13  E-value: 2.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  17 LRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLnPPH--RVKSISMTTFTQQEIEFLQKHGNEVCKQIWL 94
Cdd:cd08204    1 LEELLKLPGNKVCADCGAPDPRWASINLGVFICIRCSGIHRSL-GVHisKVRSLTLDSWTPEQVELMKAIGNARANAYYE 79

                         90       100
                 ....*....|....*....|....*..
gi 568907554  95 GLFDDRSSAIPDFRDPQKVKEFLQEKY 121
Cdd:cd08204   80 ANLPPGFKKPTPDSSDEEREQFIRAKY 106
PLN03131 PLN03131
hypothetical protein; Provisional
 7-126 1.37e-23

hypothetical protein; Provisional


Pssm-ID: 178677 [Multi-domain]  Cd Length: 705  Bit Score: 105.24  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   7 RKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNppHRVKSISMTTFTQQEIEFLQKHGN 86
Cdd:PLN03131   4 RKEEERNEKIIRGLMKLPPNRRCINCNSLGPQFVCTNFWTFICMTCSGIHREFT--HRVKSVSMSKFTSQDVEALQNGGN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568907554  87 EVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:PLN03131  82 QRAREIYLKDWDQQRQRLPDNSKVDKIREFIKDIYVDKKY 121
PLN03119 PLN03119
putative ADP-ribosylation factor GTPase-activating protein AGD14; Provisional
 7-126 4.72e-20

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


Pssm-ID: 178666  Cd Length: 648  Bit Score: 94.14  E-value: 4.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   7 RKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNppHRVKSISMTTFTQQEIEFLQKHGN 86
Cdd:PLN03119   4 KREEERNEKIIRGLMKLPPNRRCINCNSLGPQYVCTTFWTFVCMACSGIHREFT--HRVKSVSMSKFTSKEVEVLQNGGN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568907554  87 EVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:PLN03119  82 QRAREIYLKNWDHQRQRLPENSNAERVREFIKNVYVQKKY 121
ArfGap_ADAP cd08832
ArfGap with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) ...
 11-121 4.71e-16

ArfGap with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions.


Pssm-ID: 350061 [Multi-domain]  Cd Length: 113  Bit Score: 74.22  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  11 EKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLnPPH--RVKSISMTTFTQQEIEFLQKHGNEV 88
Cdd:cd08832    2 ERNKKRLLELLKLPGNNTCADCGAPDPEWASYNLGVFICLDCSGIHRSL-GTHisKVKSLRLDNWDDSQVEFMEENGNEK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568907554  89 CKQIWlglfddrSSAIPDF------RDPQKVKE-FLQEKY 121
Cdd:cd08832   81 AKAKY-------EAHVPAFyrrptpTDPQVLREqWIRAKY 113
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 8-268 1.03e-15

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


Pssm-ID: 227651 [Multi-domain]  Cd Length: 319  Bit Score: 78.28  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554   8 KQEEKHLKMLRDMtgLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHG 85
Cdd:COG5347    4 KSEDRKLLKLLKS--DSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLG-VHisKVKSLTLDNWTEEELRRMEVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  86 NEVCKQIWLGlfDDRSSAIPDFR---DPQKVKEFLQEKYEKKRWYVPPEQAKVVASvhasisgssaSSTSSTPEVKPLKS 162
Cdd:COG5347   81 NSNANRFYEK--NLLDQLLLPIKakyDSSVAKKYIRKKYELKKFIDDSSSPSDFSS----------FSASSTRTVDSVDD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554 163 LL-GESAPALHLNKGTPSQSP--VVGRSQGQQQEKKQFDLLSDL---GSDIFAAPAPQSTATANFAN--FAHFNSHAAQN 234
Cdd:COG5347  149 RLdSESQSRSSSASLGNSNRPddELNVESFQSTGSKPRSLTSTKsnkDNLLNSELLTLNSLLSSNSEvgSGTKSRSDAQE 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568907554 235 SANADFANFDAFGQSSGSSNFGGFPTASHSSFQP 268
Cdd:COG5347  229 KSSTKATESVKPGPVNTSSTSSLPPAIKRSPVQQ 262
ArfGap_SMAP2 cd08859
Stromal membrane-associated protein 2; a subfamily of the ArfGAP family; The SMAP subfamily of ...
 17-125 1.25e-15

Stromal membrane-associated protein 2; a subfamily of the ArfGAP family; The SMAP subfamily of Arf GTPase-activating proteins consists of the two structurally-related members, SMAP1 and SMAP2. Each SMAP member exhibits common and distinct functions in vesicle trafficking. They both bind to clathrin heavy chain molecules and are involved in the trafficking of clathrin-coated vesicles. SMAP1 preferentially exhibits GAP toward Arf6, while SMAP2 prefers Arf1 as a substrate. SMAP1 is involved in Arf6-dependent vesicle trafficking, but not Arf6-mediated actin cytoskeleton reorganization, and regulates clathrin-dependent endocytosis of the transferrin receptors and E-cadherin. SMAP2 regulates Arf1-dependent retrograde transport of TGN38/46 from the early endosome to the trans-Golgi network (TGN). SMAP2 has the Clathrin Assembly Lymphoid Myeloid (CALM)-binding domain, but SMAP1 does not.


Pssm-ID: 350083 [Multi-domain]  Cd Length: 107  Bit Score: 72.71  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  17 LRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQIWlg 95
Cdd:cd08859    1 LASLLLEEENKFCADCQSKGPRWASWNIGVFICIRCAGIHRNLGVHiSRVKSVNLDQWTQEQIQCMQEMGNGKANRLY-- 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568907554  96 lfddrSSAIPD-FRDPQ---KVKEFLQEKYEKKR 125
Cdd:cd08859   79 -----EAFLPEnFRRPQtdqAVEGFIRDKYEKKK 107
ArfGap_ArfGap1 cd08830
Arf1 GTPase-activating protein 1; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 15-91 4.36e-13

Arf1 GTPase-activating protein 1; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif.


Pssm-ID: 350059 [Multi-domain]  Cd Length: 115  Bit Score: 65.98  E-value: 4.36e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568907554  15 KMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPHR--VKSISMTTFTQQEIEFLQKHGNEVCKQ 91
Cdd:cd08830    3 AVLRELQKLPGNNRCFDCGAPNPQWASVSYGIFICLECSGVHRGLG-VHIsfVRSITMDSWSEKQLKKMELGGNAKLRE 80
ArfGap_SMAP cd08839
Stromal membrane-associated proteins; a subfamily of the ArfGAP family; The SMAP subfamily of ...
 17-121 4.38e-13

Stromal membrane-associated proteins; a subfamily of the ArfGAP family; The SMAP subfamily of Arf GTPase-activating proteins consists of the two structurally-related members, SMAP1 and SMAP2. Each SMAP member exhibits common and distinct functions in vesicle trafficking. They both bind to clathrin heavy chain molecules and are involved in the trafficking of clathrin-coated vesicles. SMAP1 preferentially exhibits GAP toward Arf6, while SMAP2 prefers Arf1 as a substrate. SMAP1 is involved in Arf6-dependent vesicle trafficking, but not Arf6-mediated actin cytoskeleton reorganization, and regulates clathrin-dependent endocytosis of the transferrin receptors and E-cadherin. SMAP2 regulates Arf1-dependent retrograde transport of TGN38/46 from the early endosome to the trans-Golgi network (TGN). SMAP2 has the Clathrin Assembly Lymphoid Myeloid (CALM)-binding domain, but SMAP1 does not.


Pssm-ID: 350068 [Multi-domain]  Cd Length: 103  Bit Score: 65.37  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  17 LRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNEVCKQIWl 94
Cdd:cd08839    1 LAKLLREEDNKYCADCGAKGPRWASWNLGVFICIRCAGIHRNLG-VHisKVKSVNLDSWTPEQVQSMQEMGNARANAYY- 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568907554  95 glfddrSSAIPD-FRDPQ---KVKEFLQEKY 121
Cdd:cd08839   79 ------EANLPDgFRRPQtdsALENFIRDKY 103
ArfGap_ADAP1 cd08843
ADAP1 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs ...
 10-121 1.07e-12

ADAP1 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions.


Pssm-ID: 350069 [Multi-domain]  Cd Length: 112  Bit Score: 64.64  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  10 EEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVC 89
Cdd:cd08843    1 GKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVEFMASHGNDAA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568907554  90 KqiwlGLFDDRSSAI---PDFRDPQKVKE-FLQEKY 121
Cdd:cd08843   81 R----ARFESKVPSFyyrPTPSDCQLLREqWIRAKY 112
ArfGap_ArfGap1_like cd08959
ARF1 GTPase-activating protein 1-like; ArfGAP (ADP Ribosylation Factor GTPase Activating ...
 15-91 1.76e-12

ARF1 GTPase-activating protein 1-like; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif.


Pssm-ID: 350084 [Multi-domain]  Cd Length: 115  Bit Score: 64.07  E-value: 1.76e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568907554  15 KMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPHR--VKSISMTTFTQQEIEFLQKHGNEVCKQ 91
Cdd:cd08959    3 AVFKKLRSKPENKVCFDCGAKNPQWASVTYGIFICLDCSGVHRGLG-VHIsfVRSTTMDKWTEEQLRKMKVGGNANARE 80
ArfGap_ArfGap2_3_like cd08831
Arf1 GTPase-activating protein 2/3-like; ArfGAP (ADP Ribosylation Factor GTPase Activating ...
 24-87 1.10e-11

Arf1 GTPase-activating protein 2/3-like; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif.


Pssm-ID: 350060 [Multi-domain]  Cd Length: 116  Bit Score: 61.79  E-value: 1.10e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568907554  24 PHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNE 87
Cdd:cd08831   13 PENKVCFDCGAKNPTWASVTFGVFLCLDCSGVHRSLG-VHisFVRSTNLDSWTPEQLRRMKVGGNA 77
ArfGap_ADAP2 cd08844
ADAP2 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs ...
 11-90 1.88e-11

ADAP2 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions.


Pssm-ID: 350070 [Multi-domain]  Cd Length: 112  Bit Score: 60.94  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  11 EKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCK 90
Cdd:cd08844    2 DRNKKRLLELLKLPGNSVCADCGAPDPDWASYTLGIFICLNCSGVHRNLPDISRVKSIRLDFWEDELVEFMKENGNLKAK 81
ArfGap_AGAP2 cd08853
ArfGAP with GTPase domain, ANK repeat and PH domain 2; The AGAP subfamily of ADP-ribosylation ...
 14-122 5.80e-10

ArfGAP with GTPase domain, ANK repeat and PH domain 2; The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking.


Pssm-ID: 350078 [Multi-domain]  Cd Length: 109  Bit Score: 56.94  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  14 LKMLRDMTGlphNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08853    4 LQSIRNMRG---NSHCVDCETQNPKWASLNLGVLMCIECSGIHRNLGTHlSRVRSLDLDDWPVELRKVMSSIGNELANSI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568907554  93 WLGlfDDRSSAIPDFRDPQKVKE-FLQEKYE 122
Cdd:cd08853   81 WEG--SSQGQTKPSSDSTREEKErWIRAKYE 109
ArfGap_ARAP cd08837
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing proteins; The ARAP subfamily ...
 24-126 7.59e-09

ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing proteins; The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics.


Pssm-ID: 350066 [Multi-domain]  Cd Length: 116  Bit Score: 53.92  E-value: 7.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  24 PHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTT--FTQQEIEFLQKHGNEVCKQIWLGLFDDr 100
Cdd:cd08837   11 PANRFCADCGAPDPDWASINLCVVICKQCAGEHRSLGSNiSKVRSLKMDTkvWTEELVELFLKLGNDRANRFWAANLPP- 89

                         90       100
                 ....*....|....*....|....*.
gi 568907554 101 SSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:cd08837   90 SEALHPDADSEQRREFITAKYREGKY 115
ArfGap_AGAP1 cd08854
ArfGAP with GTPase domain, ANK repeat and PH domain 1; The AGAP subfamily of ADP-ribosylation ...
 14-122 2.20e-08

ArfGAP with GTPase domain, ANK repeat and PH domain 1; The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking.


Pssm-ID: 350079 [Multi-domain]  Cd Length: 109  Bit Score: 52.32  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  14 LKMLRDMTGlphNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08854    4 IQAIRNAKG---NSLCVDCGAPNPTWASLNLGALICIECSGIHRNLGTHlSRVRSLDLDDWPRELTLVLTAIGNHMANSI 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 568907554  93 WLGLFDDRSSAIPDFRDPQKvKEFLQEKYE 122
Cdd:cd08854   81 WESCTQGRTKPAPDSSREER-ESWIRAKYE 109
ArfGap_ACAP3 cd08850
ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domains 3); ACAP3 belongs ...
 16-126 2.54e-08

ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domains 3); ACAP3 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. It has been shown that ACAP3 positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) also have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages.


Pssm-ID: 350075 [Multi-domain]  Cd Length: 116  Bit Score: 52.25  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  16 MLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:cd08850    3 ILQRVQSIAGNDQCCDCGQPDPRWASINLGILLCIECSGIHRSLG-VHcsKVRSLTLDSWEPELLKLMCELGNSTVNQIY 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568907554  94 LGLFDDRSSAIPDFRDPQKVKE-FLQEKYEKKRW 126
Cdd:cd08850   82 EAQCEELGLKKPTASSSRQDKEaWIKAKYVEKKF 115
ArfGap_AGAP3 cd08855
ArfGAP with GTPase domain, ANK repeat and PH domain 3; The AGAP subfamily of ADP-ribosylation ...
 14-122 7.51e-08

ArfGAP with GTPase domain, ANK repeat and PH domain 3; The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion.


Pssm-ID: 350080 [Multi-domain]  Cd Length: 110  Bit Score: 50.82  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  14 LKMLRDMTGlphNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQI 92
Cdd:cd08855    5 IQSIRNVRG---NSFCIDCDAPNPDWASLNLGALMCIECSGIHRNLGTHlSRVRSLDLDDWPVELSMVMTAIGNAMANSV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 568907554  93 WLGLFDDRSSAIPDFRDPQKvKEFLQEKYE 122
Cdd:cd08855   82 WEGALDGYSKPGPDSTREEK-ERWIRAKYE 110
ArfGap_ACAP2 cd08851
ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domains 2); ACAP2 belongs ...
 17-126 9.88e-08

ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domains 2); ACAP2 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons.


Pssm-ID: 350076 [Multi-domain]  Cd Length: 116  Bit Score: 50.75  E-value: 9.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  17 LRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLG 95
Cdd:cd08851    4 LQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHfSKVRSLTLDTWEPELLKLMCELGNDVINRIYEA 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568907554  96 LFDDRSSAIPDFRDPQKVKE-FLQEKY-EKKRW 126
Cdd:cd08851   84 RVEKMGAKKPQPGGQRQEKEaYIRAKYvERKFV 116
ArfGap_ARAP1 cd17901
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 1; The ARAP subfamily ...
 24-126 1.10e-07

ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 1; The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP1 localizes to the plasma membrane, the Golgi complex, and endosomal compartments. It displays PI(3,4,5)P3-dependent ArfGAP activity that regulates Arf-, RhoA-, and Cdc42-dependent cellular events. For example, ARAP1 inhibits the trafficking of epidermal growth factor receptor (EGFR) to the early endosome.


Pssm-ID: 350088 [Multi-domain]  Cd Length: 116  Bit Score: 50.58  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  24 PHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISM--TTFTQQEIEFLQKHGNEVCKQIWlGLFDDR 100
Cdd:cd17901   11 ESNRFCADCGSPKPDWASVNLCVVICKRCAGEHRGLGPSvSKVRSLKMdrKVWTEELIELFLLLGNGKANQFW-AANVPP 89

                         90       100
                 ....*....|....*....|....*.
gi 568907554 101 SSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:cd17901   90 SEALCPSSSSEERRHFITAKYKEGKY 115
ArfGap_ARAP2 cd08856
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 2; The ARAP subfamily ...
 26-126 2.87e-07

ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 2; The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP2 localizes to the cell periphery and on focal adhesions composed of paxillin and vinculin, and functions downstream of RhoA to regulate focal adhesion dynamics. ARAP2 is a PI(3,4,5)P3-dependent Arf6 GAP that binds RhoA-GTP, but it lacks the predicted catalytic arginine in the RhoGAP domain and does not have RhoGAP activity. ARAP2 reduces Rac1oGTP levels by reducing Arf6oGTP levels through GAP activity. AGAP2 also binds to and regulates focal adhesion kinase (FAK). Thus, ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology.


Pssm-ID: 350081 [Multi-domain]  Cd Length: 121  Bit Score: 49.52  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  26 NRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISM--TTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSS 102
Cdd:cd08856   18 NRSCADCKAPDPDWASINLCVVICKKCAGQHRSLGPKdSKVRSLKMdaSIWSNELIELFIVVGNKPANLFWAANLFSEED 97

                         90       100
                 ....*....|....*....|....
gi 568907554 103 AIPDfRDPQKVKEFLQEKYEKKRW 126
Cdd:cd08856   98 LHMD-SDVEQRTPFITQKYKEGKF 120
ArfGap_ACAP1 cd08852
ArfGAP domain of ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domains 1); ACAP1 belongs ...
 23-126 3.13e-07

ArfGAP domain of ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domains 1); ACAP1 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons.


Pssm-ID: 350077 [Multi-domain]  Cd Length: 120  Bit Score: 49.19  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  23 LPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDR 100
Cdd:cd08852   10 VDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLG-VHfsKVRSLTLDSWEPELVKLMCELGNVIINQIYEARIEAM 88

                         90       100
                 ....*....|....*....|....*..
gi 568907554 101 SSAIPDFRDPQKVKE-FLQEKYEKKRW 126
Cdd:cd08852   89 AIKKPGPSSSRQEKEaWIRAKYVEKKF 115
ArfGap_AGAP cd08836
ArfGAP with GTPase domain, ANK repeat and PH domains; The AGAP subfamily of ADP-ribosylation ...
 14-122 4.02e-07

ArfGAP with GTPase domain, ANK repeat and PH domains; The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking.


Pssm-ID: 350065 [Multi-domain]  Cd Length: 108  Bit Score: 48.44  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  14 LKMLRDMTGlphNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNEVCKQ 91
Cdd:cd08836    3 LQAIRNVRG---NDHCVDCGAPNPDWASLNLGALMCIECSGIHRNLG-THisRVRSLDLDDWPVELLKVMSAIGNDLANS 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568907554  92 IWLGLFDDRSSaiPDFRDPQKVKE-FLQEKYE 122
Cdd:cd08836   79 VWEGNTQGRTK--PTPDSSREEKErWIRAKYE 108
ArfGap_ASAP cd08834
ArfGAP domain of ASAP (Arf GAP, SH3, ANK repeat and PH domains) subfamily of ADP-ribosylation ...
 17-125 4.27e-07

ArfGAP domain of ASAP (Arf GAP, SH3, ANK repeat and PH domains) subfamily of ADP-ribosylation factor GTPase-activating proteins; The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. Both ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma.


Pssm-ID: 350063 [Multi-domain]  Cd Length: 117  Bit Score: 48.76  E-value: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  17 LRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPH-RVKSISMTTFTQQEIEFLQKHGNEVCKQIWLG 95
Cdd:cd08834    6 IAEVKRLPGNDVCCDCGSPDPTWLSTNLGILTCIECSGVHRELGVHVsRIQSLTLDNLGTSELLLARNLGNEGFNEIMEA 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 568907554  96 LFDDRSSAIPDFRDPQKvKEFLQEKYEKKR 125
Cdd:cd08834   86 NLPPGYKPTPNSDMEER-KDFIRAKYVEKK 114
ArfGap_ArfGap3 cd09028
Arf1 GTPase-activating protein 3; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 16-59 1.54e-06

Arf1 GTPase-activating protein 3; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif.


Pssm-ID: 350085 [Multi-domain]  Cd Length: 120  Bit Score: 47.37  E-value: 1.54e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568907554  16 MLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGL 59
Cdd:cd09028    9 IFKRLRSVPTNKVCFDCGAKNPSWASITYGVFLCIDCSGIHRSL 52
ArfGap_ArfGap2 cd09029
Arf1 GTPase-activating protein 2; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 16-59 6.10e-06

Arf1 GTPase-activating protein 2; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif.


Pssm-ID: 350086 [Multi-domain]  Cd Length: 120  Bit Score: 45.82  E-value: 6.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568907554  16 MLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGL 59
Cdd:cd09029    9 LFKRLRAIPTNKACFDCGAKNPSWASITYGVFLCIDCSGVHRSL 52
ArfGap_ASAP1 cd08848
ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein 1); ...
 16-126 6.42e-06

ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein 1); The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma.


Pssm-ID: 350073 [Multi-domain]  Cd Length: 122  Bit Score: 45.80  E-value: 6.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  16 MLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQIWL 94
Cdd:cd08848    5 IIDDVQRLPGNEVCCDCGSPDPTWLSTNLGILTCIECSGIHREMGVHiSRIQSLELDKLGTSELLLAKNVGNNSFNDIME 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568907554  95 GLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRW 126
Cdd:cd08848   85 GNLPSPSPKPSPSSDMTARKEYITAKYVEHRF 116
ArfGap_ASAP2 cd08849
ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain, ANK repeat and PH domain-containing protein 2) ...
 15-126 1.14e-05

ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain, ANK repeat and PH domain-containing protein 2); The Arf GAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf , thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport.


Pssm-ID: 350074 [Multi-domain]  Cd Length: 123  Bit Score: 44.97  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  15 KMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPH-RVKSISMTTFTQQEIEFLQKHGNEVCKQIW 93
Cdd:cd08849    4 EIISEVQRMTGNDVCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVHYsRMQSLTLDVLGTSELLLAKNIGNAGFNEIM 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568907554  94 LGLFDDRSSAIPD-FRDPQKVKEFLQEKYEKKRW 126
Cdd:cd08849   84 EACLPAEDVVKPNpGSDMNARKDYITAKYIERRY 117
ArfGap_ACAP cd08835
ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins; ArfGAP ...
 11-125 1.56e-05

ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins; ArfGAP domain is an essential part of ACAP proteins that play important role in endocytosis, actin remodeling and receptor tyrosine kinase-dependent cell movement. ACAP subfamily of ArfGAPs are composed of coiled coils (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. In addition, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons.


Pssm-ID: 350064 [Multi-domain]  Cd Length: 116  Bit Score: 44.17  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  11 EKHLKMLRDmtgLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNpPH--RVKSISMTTFTQQEIEFLQKHGNEV 88
Cdd:cd08835    1 GSALEQVLS---VPGNAQCCDCGSPDPRWASINLGVTLCIECSGIHRSLG-VHvsKVRSLTLDSWEPELLKVMLELGNDV 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568907554  89 CKQIWLGLFDDRSSAIPDFRDPQKVKE-FLQEKYEKKR 125
Cdd:cd08835   77 VNRIYEANVPDDGSVKPTPDSSRQEREaWIRAKYVEKK 114
ArfGap_GIT cd08833
The GIT subfamily of ADP-ribosylation factor GTPase-activating proteins; The GIT (G-protein ...
 20-121 4.59e-05

The GIT subfamily of ADP-ribosylation factor GTPase-activating proteins; The GIT (G-protein coupled receptor kinase-interacting protein) subfamily includes GIT1 and GIT2, which have three ANK repeats, a Spa-homology domain (SHD), a coiled-coil domain and a C-terminal paxillin-binding site (PBS). The GIT1/2 proteins are GTPase-activating proteins that function as an inactivator of Arf signaling, and interact with the PIX/Cool family of Rac/Cdc42 guanine nucleotide exchange factors (GEFs). Unlike other ArfGAPs, GIT and PIX (Pak-interacting exchange factor) proteins are tightly associated to form an oligomeric complex that acts as a scaffold and signal integrator that can be recruited for multiple signaling pathways. The GIT/PIX complex functions as a signaling scaffold by binding to specific protein partners. As a result, the complex is transported to specific cellular locations. For instance, the GIT partners paxillin or integrin-alpha4 (to focal adhesions), piccolo and liprin-alpha (to synapses), and the beta-PIX partner Scribble (to epithelial cell-cell contacts and synapses). Moreover, the GIT/PIT complex functions to integrate signals from multiple GTP-binding protein and protein kinase pathways to regulate the actin cytoskeleton and thus cell polarity, adhesion and migration.


Pssm-ID: 350062 [Multi-domain]  Cd Length: 109  Bit Score: 42.67  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  20 MTGLPHNRK-CFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGNEVCKQIW-LGL 96
Cdd:cd08833    1 IRGKSSNARvCADCSAPDPEWASINRGVLICDECCSIHRSLGRHiSQVKSLRKDQWPPSLLEMVQTLGNNGANSIWeHSL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 568907554  97 FDDRSSAI-----PDFRDPQKvKEFLQEKY 121
Cdd:cd08833   81 LDPSQSGKrkpipPDPVHPTK-EEFIKAKY 109
ArfGap_ARAP3 cd17902
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 3; The ARAP subfamily ...
 24-126 6.75e-05

ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 3; The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP3 possesses a unique dual-specificity GAP activity for Arf6 and RhoA regulated by PI(3,4,5)P3 and a small GTPase Rap1-GTP. The RhoGAP activity of ARAP3 is enhanced by direct binding of Rap1-GTP to the Ras-association (RA) domain. ARAP3 is involved in regulation of cell shape and adhesion.


Pssm-ID: 350089 [Multi-domain]  Cd Length: 116  Bit Score: 42.59  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  24 PHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTT--FTQQEIEFLQKHGNEVCKQIWLGLFDDR 100
Cdd:cd17902   11 KANRFCADCHASSPDWASINLCVVICKQCAGQHRSLGSGiSKVQSLKLDTsvWSNEIVQLFIVLGNDRANRFWAARLPAS 90

                         90       100
                 ....*....|....*....|....*.
gi 568907554 101 SSAIPDfRDPQKVKEFLQEKYEKKRW 126
Cdd:cd17902   91 EALHPD-ATPEQRREFISRKYREGRF 115
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 385-575 2.81e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.80  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  385 SSAATSSNAYTPTSNASSSVFGTVPVGASAQTQPASSgpAPFGATPSTNPFVAATGPSAASSTNpfqTNARGATGLSGAM 464
Cdd:pfam17823 107 ADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFS--APRAAACRANASAAPRAAIAAASAP---HAASPAPRTAASS 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  465 HSQVFPHAHFAATFGTASMSMPAGFgTPAQySLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGA-GFATFGQTKPVVTP 543
Cdd:pfam17823 182 TTAASSTTAASSAPTTAASSAPATL-TPAR-GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAvGTVTPAALATLAAA 259

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568907554  544 FGQVAAAGVSSNP----FMTGAPTGQLPTGSSSTNP 575
Cdd:pfam17823 260 AGTVASAAGTINMgdphARRLSPAKHMPSDTMARNP 295
PLN03114 PLN03114
ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
 14-86 1.61e-03

ADP-ribosylation factor GTPase-activating protein AGD10; Provisional


Pssm-ID: 178661 [Multi-domain]  Cd Length: 395  Bit Score: 40.99  E-value: 1.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568907554  14 LKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPP-HRVKSISMTTFTQQEIEFLQKHGN 86
Cdd:PLN03114  10 ISVFKKLKAKSDNKICFDCNAKNPTWASVTYGIFLCIDCSAVHRSLGVHiSFVRSTNLDSWSSEQLKMMIYGGN 83
ArfGap_ASAP3 cd17900
ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and PH domain-containing protein 3); The ...
 23-126 2.84e-03

ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and PH domain-containing protein 3); The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP1 and ASAP2, ASAP3 do not have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma.


Pssm-ID: 350087 [Multi-domain]  Cd Length: 124  Bit Score: 37.90  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568907554  23 LPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPH-RVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRS 101
Cdd:cd17900   12 RPGNSQCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVRYsRIQSLTLDLLSTSELLLAVSMGNTRFNEVMEATLPAHG 91

                         90       100
                 ....*....|....*....|....*.
gi 568907554 102 SAIPDFR-DPQKVKEFLQEKYEKKRW 126
Cdd:cd17900   92 GPKPSAEsDMGTRKDYIMAKYVEHRF 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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