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Conserved domains on  [gi|1143464692|ref|NP_001335541|]
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ANK_REP_REGION domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArfGap super family cl28907
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 1-62 4.20e-22

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.


The actual alignment was detected with superfamily member cd08835:

Pssm-ID: 355783 [Multi-domain]  Cd Length: 116  Bit Score: 89.24  E-value: 4.20e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSivpPQINEKSARPAREAWIKAKYVERRFA 62
Cdd:cd08835    58 LDSWEPELLKVMLELGNDVVNRIYEANVPDDGS---VKPTPDSSRQEREAWIRAKYVEKKFV 116
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-272 3.60e-20

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 3.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 162 EACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQL 240
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1143464692 241 LKRGADSNLANVDSKTPLDIAMECTHADIVTL 272
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
 
Name Accession Description Interval E-value
ArfGap_ACAP cd08835
ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins; ArfGAP ...
 1-62 4.20e-22

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: 89.24  E-value: 4.20e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSivpPQINEKSARPAREAWIKAKYVERRFA 62
Cdd:cd08835    58 LDSWEPELLKVMLELGNDVVNRIYEANVPDDGS---VKPTPDSSRQEREAWIRAKYVEKKFV 116
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-272 3.60e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 3.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 162 EACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQL 240
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1143464692 241 LKRGADSNLANVDSKTPLDIAMECTHADIVTL 272
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-272 3.17e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 192 LHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTlPVCQLLKRGADSNLANvDSKTPLDIAMECTHADIVT 271
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  .
gi 1143464692 272 L 272
Cdd:pfam12796  79 L 79
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 1-65 4.84e-13

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: 64.55  E-value: 4.84e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPqinekSARPAREAWIKAKYVERRFAVAE 65
Cdd:pfam01412  58 LDTWTDEQLELMKAGGNDRANEFWEANLPPSYKPPPS-----SDREKRESFIRAKYVEKKFAKPG 117
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 125-292 1.13e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 125 PVPTASKRLSACGS-----DTNLDAIGSSSIDTKTVEWDSVKEacecgdllalmtayaQGFDLNALHNGTTALHIATRNG 199
Cdd:PTZ00322   29 AKPISFERMAAIQEeiariDTHLEALEATENKDATPDHNLTTE---------------EVIDPVVAHMLTVELCQLAASG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 200 QTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLFrVTIMR 279
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL-SRHSQ 172

                         170
                  ....*....|...
gi 1143464692 280 NDFNADFNNPMDE 292
Cdd:PTZ00322  173 CHFELGANAKPDS 185
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 187-216 3.63e-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 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1143464692  187 NGTTALHIATRNGQTAAVEFLLLNGAKINM 216
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ArfGap_ACAP cd08835
ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins; ArfGAP ...
 1-62 4.20e-22

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: 89.24  E-value: 4.20e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSivpPQINEKSARPAREAWIKAKYVERRFA 62
Cdd:cd08835    58 LDSWEPELLKVMLELGNDVVNRIYEANVPDDGS---VKPTPDSSRQEREAWIRAKYVEKKFV 116
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-272 3.60e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 3.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 162 EACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQL 240
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1143464692 241 LKRGADSNLANVDSKTPLDIAMECTHADIVTL 272
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
167-272 6.48e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 6.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 167 GDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGA 245
Cdd:COG0666    65 GDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144

                          90       100
                  ....*....|....*....|....*..
gi 1143464692 246 DSNLANVDSKTPLDIAMECTHADIVTL 272
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKL 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
163-288 1.76e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 163 ACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLL 241
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1143464692 242 KRGADSNLANVDSKTPLDIAMECTHADIVTLFRVTIMRNDFNADFNN 288
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-272 3.17e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 192 LHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTlPVCQLLKRGADSNLANvDSKTPLDIAMECTHADIVT 271
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  .
gi 1143464692 272 L 272
Cdd:pfam12796  79 L 79
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 1-65 4.84e-13

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: 64.55  E-value: 4.84e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPqinekSARPAREAWIKAKYVERRFAVAE 65
Cdd:pfam01412  58 LDTWTDEQLELMKAGGNDRANEFWEANLPPSYKPPPS-----SDREKRESFIRAKYVEKKFAKPG 117
Ank_2 pfam12796
Ankyrin repeats (3 copies);
163-251 3.28e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 163 ACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEfLLLNGAKINMLDEKlNTPLHLAAKEGHTLPVCQLL 241
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNG-RTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1143464692 242 KRGADSNLAN 251
Cdd:pfam12796  82 EKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 125-292 1.13e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 125 PVPTASKRLSACGS-----DTNLDAIGSSSIDTKTVEWDSVKEacecgdllalmtayaQGFDLNALHNGTTALHIATRNG 199
Cdd:PTZ00322   29 AKPISFERMAAIQEeiariDTHLEALEATENKDATPDHNLTTE---------------EVIDPVVAHMLTVELCQLAASG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 200 QTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLFrVTIMR 279
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL-SRHSQ 172

                         170
                  ....*....|...
gi 1143464692 280 NDFNADFNNPMDE 292
Cdd:PTZ00322  173 CHFELGANAKPDS 185
ArfGap cd08204
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 1-56 3.18e-10

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: 56.35  E-value: 3.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPQinekSARPAREAWIKAKY 56
Cdd:cd08204    55 LDSWTPEQVELMKAIGNARANAYYEANLPPGFKKPTPD----SSDEEREQFIRAKY 106
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 146-272 1.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 146 GSSSIDTKTVEWDSVKEACEcGDLLALMTAYAQGFDLNALHNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPL 225
Cdd:PHA02878  127 NIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPL 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1143464692 226 HLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAM-ECTHADIVTL 272
Cdd:PHA02878  206 HHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKL 253
ArfGap_ASAP cd08834
ArfGAP domain of ASAP (Arf GAP, SH3, ANK repeat and PH domains) subfamily of ADP-ribosylation ...
 1-63 3.19e-08

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: 51.07  E-value: 3.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143464692   1 MDSI-DNELRdVLLALGNRQVNEIFLAHLPPadsivPPQINEKSARPAREAWIKAKYVERRFAV 63
Cdd:cd08834    60 LDNLgTSELL-LARNLGNEGFNEIMEANLPP-----GYKPTPNSDMEERKDFIRAKYVEKKFVV 117
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 180-269 3.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 180 FDLNALHNGTTALHIATRNGQTAAVefLLLNGAKINMLDEKLNTPLHLAA--KEGHTLPVCQLLKRGADSNLANVDSKTP 257
Cdd:PHA03100   67 NNSTPLHYLSNIKYNLTDVKEIVKL--LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENL 144

                          90
                  ....*....|..
gi 1143464692 258 LDIAMECTHADI 269
Cdd:PHA03100  145 LHLYLESNKIDL 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
168-273 4.08e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 168 DLLALMTAYAQGFDLNALHNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADS 247
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100
                  ....*....|....*....|....*.
gi 1143464692 248 NLANVDSKTPLDIAMECTHADIVTLF 273
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 169-272 5.26e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 169 LLALMTAyaqGFDLNALH-NGTTALHIATRNGQTAAV-EFLLLNGAKINMLDEKLNTPLH--LAAKEGHTLPVCQLLKRG 244
Cdd:PHA03095   66 VRLLLEA---GADVNAPErCGFTPLHLYLYNATTLDViKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG 142

                          90       100
                  ....*....|....*....|....*...
gi 1143464692 245 ADSNLANVDSKTPLDIAMECTHADIVTL 272
Cdd:PHA03095  143 ADVNALDLYGMTPLAVLLKSRNANVELL 170
ArfGap_ACAP3 cd08850
ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domains 3); ACAP3 belongs ...
 1-61 8.80e-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: 49.94  E-value: 8.80e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPpqiNEKSARPAREAWIKAKYVERRF 61
Cdd:cd08850    58 LDSWEPELLKLMCELGNSTVNQIYEAQCEELGLKKP---TASSSRQDKEAWIKAKYVEKKF 115
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-273 1.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 204 VEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLF 273
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
 188-273 2.13e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 188 GTTALHIATRNGQTAA--VEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECT 265
Cdd:PHA03095  222 GNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301


                  ....*...
gi 1143464692 266 HADIVTLF 273
Cdd:PHA03095  302 NGRAVRAA 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
188-241 4.45e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 4.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1143464692 188 GTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHtLPVCQLL 241
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN-VEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 121-313 1.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 121 DLSV-PVPTASKR----LSACGSDTNLdaigsSSIDTKTVEWDSVKEacecGDLLALMTAYAQGFDLNALH-NGTTALHI 194
Cdd:PHA02874   93 DTSIlPIPCIEKDmiktILDCGIDVNI-----KDAELKTFLHYAIKK----GDLESIKMLFEYGADVNIEDdNGCYPIHI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 195 ATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEG-------------------------------HTLPVCQLLKR 243
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdyacikllidhgnhimnkckngftplhnaiiHNRSAIELLIN 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143464692 244 GADSNLANVDSKTPLDIAME--CTH--ADIVTLFRVTIMRNDFNADfnNPMDETVE-----AVISDIARRAATEKEQKK 313
Cdd:PHA02874  244 NASINDQDIDGSTPLHHAINppCDIdiIDILLYHKADISIKDNKGE--NPIDTAFKyinkdPVIKDIIANAVLIKEADK 320
ArfGap_ACAP1 cd08852
ArfGAP domain of ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domains 1); ACAP1 belongs ...
 1-61 1.98e-06

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: 46.11  E-value: 1.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLppaDSIVPPQINEKSARPAREAWIKAKYVERRF 61
Cdd:cd08852    58 LDSWEPELVKLMCELGNVIINQIYEARI---EAMAIKKPGPSSSRQEKEAWIRAKYVEKKF 115
ArfGap_ASAP3 cd17900
ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and PH domain-containing protein 3); The ...
 10-67 2.25e-06

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: 45.99  E-value: 2.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692  10 DVLLAL--GNRQVNEIFLAHLPPADSIVPpqiNEKSARPAREAWIKAKYVERRFAVAEDT 67
Cdd:cd17900    67 ELLLAVsmGNTRFNEVMEATLPAHGGPKP---SAESDMGTRKDYIMAKYVEHRFVRKRCT 123
ArfGap_ACAP2 cd08851
ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domains 2); ACAP2 belongs ...
 1-61 3.38e-06

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: 45.36  E-value: 3.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPQineKSARPAREAWIKAKYVERRF 61
Cdd:cd08851    58 LDTWEPELLKLMCELGNDVINRIYEARVEKMGAKKPQP---GGQRQEKEAYIRAKYVERKF 115
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-261 7.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.60e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1143464692 214 INMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIA 261
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 179-263 1.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 179 GFDLNALHNGT-TALHIATRNGQT-AAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQ-LLKRGADSNLANVDSK 255
Cdd:PHA02876  398 GADIEALSQKIgTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEmLLDNGADVNAINIQNQ 477


                  ....*...
gi 1143464692 256 TPLDIAME 263
Cdd:PHA02876  478 YPLLIALE 485
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 205-283 1.78e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 205 EFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLF---RVTIMRND 281
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidnRSNINKND 241


                  ..
gi 1143464692 282 FN 283
Cdd:PHA02876  242 LS 243
Ank_4 pfam13637
Ankyrin repeats (many copies);
156-208 1.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1143464692 156 EWDSVKEACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLL 208
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-273 2.76e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 2.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1143464692 225 LHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLF 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ArfGap_ASAP2 cd08849
ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain, ANK repeat and PH domain-containing protein 2) ...
 10-62 4.38e-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: 42.27  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1143464692  10 DVLLA--LGNRQVNEIFLAHLPPADSIVPpqiNEKSARPAREAWIKAKYVERRFA 62
Cdd:cd08849    67 ELLLAknIGNAGFNEIMEACLPAEDVVKP---NPGSDMNARKDYITAKYIERRYA 118
Ank_5 pfam13857
Ankyrin repeats (many copies);
181-228 4.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1143464692 181 DLNALHN-GTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLA 228
Cdd:pfam13857   8 DLNRLDGeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-287 5.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 204 VEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLP-----VCQLLKRGADSNLANVDSKTPLDIAMECT--HADIVTLFRvt 276
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLL-- 128

                          90
                  ....*....|.
gi 1143464692 277 imrnDFNADFN 287
Cdd:PHA03100  129 ----DNGANVN 135
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 178-261 9.78e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 178 QGFDLNALH-NGTTALHIATRNG-QTAAVEFLLLNGAKINMLDEKLNTPLHLAAK-EGHTLPVCQLLKRGADSNLANVDS 254
Cdd:PHA02876  296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCD 375


                  ....*..
gi 1143464692 255 KTPLDIA 261
Cdd:PHA02876  376 KTPIHYA 382
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
163-258 1.54e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 163 ACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLL 241
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                          90
                  ....*....|....*..
gi 1143464692 242 KRGADSNLANVDSKTPL 258
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-273 1.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 185 LHNG--TTALHIATRNGQTaaVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAM 262
Cdd:PHA02874   88 IDNGvdTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165

                          90
                  ....*....|.
gi 1143464692 263 ECTHADIVTLF 273
Cdd:PHA02874  166 KHNFFDIIKLL 176
ArfGap_ARAP cd08837
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing proteins; The ARAP subfamily ...
 6-61 1.99e-04

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: 40.44  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1143464692   6 NELRDVLLALGNRQVNEIFLAHLPPADSIVPpqineKSARPAREAWIKAKYVERRF 61
Cdd:cd08837    65 EELVELFLKLGNDRANRFWAANLPPSEALHP-----DADSEQRREFITAKYREGKY 115
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 164-281 2.19e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 164 CECGDLLALMTAYAQGFDLNAL------HNGTTALHIATRNGQTAAVEFLLLN---GAKINMLDEKL-NTPLHLAAK-EG 232
Cdd:PHA02736   25 CRNGGVTDLLAFKNAISDENRYlvleynRHGKQCVHIVSNPDKADPQEKLKLLmewGADINGKERVFgNTPLHIAVYtQN 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1143464692 233 HTLP--VCQllKRGADSNLANVDSKTPLDIAMECTHADIVTLFRVTIMRND 281
Cdd:PHA02736  105 YELAtwLCN--QPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153
PHA02946 PHA02946
ankyin-like protein; Provisional
 204-292 2.38e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 204 VEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLdIAMECTHADIVTLFRVTImrnDFN 283
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL-YYLSGTDDEVIERINLLV---QYG 130


                  ....*....
gi 1143464692 284 ADFNNPMDE 292
Cdd:PHA02946  131 AKINNSVDE 139
ArfGap_ARAP3 cd17902
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 3; The ARAP subfamily ...
 6-61 3.73e-04

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: 39.51  E-value: 3.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1143464692   6 NELRDVLLALGNRQVNEIFLAHLPPADSIVPpqinEKSARPAREaWIKAKYVERRF 61
Cdd:cd17902    65 NEIVQLFIVLGNDRANRFWAARLPASEALHP----DATPEQRRE-FISRKYREGRF 115
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 188-262 5.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 5.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143464692 188 GTTALHIAT-RNGQTAAVEFLLLNGAKINMLDEKLN-TPLHLAAKEGHTLPVcqLLKRGADSNLANVDSKTPLDIAM 262
Cdd:PHA02878  234 GNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 168-308 5.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 168 DLLALMTAYAQGFDLNALhNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTlPVCQ-LLKRGAD 246
Cdd:PHA02875  116 DIMKLLIARGADPDIPNT-DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI-AICKmLLDSGAN 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143464692 247 SN-LANVDSKTPLDIAMECTHADIVTLFR--------VTIMRNDFNADFN-------NPMDETVEAVISDIARRAATE 308
Cdd:PHA02875  194 IDyFGKNGCVAALCYAIENNKIDIVRLFIkrgadcniMFMIEGEECTILDmicnmctNLESEAIDALIADIAIRIHKK 271
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 158-237 6.85e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 158 DSVKEACECGDLLALMTAYAQGFDLNAL-HNGTTALHIATRNGQTAAVEFLLLNGA---KINMLDEKLNTPLH--LAAKE 231
Cdd:PLN03192  624 DLLCTAAKRNDLTAMKELLKQGLNVDSEdHQGATALQVAMAEDHVDMVRLLIMNGAdvdKANTDDDFSPTELRelLQKRE 703


                  ....*..
gi 1143464692 232 -GHTLPV 237
Cdd:PLN03192  704 lGHSITI 710
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 187-219 8.71e-04

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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 8.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1143464692 187 NGTTALHIA-TRNGQTAAVEFLLLNGAKINMLDE 219
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 190-216 1.09e-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: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*..
gi 1143464692 190 TALHIATRNGQTAAVEFLLLNGAKINM 216
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ArfGap_ASAP1 cd08848
ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein 1); ...
 10-62 1.37e-03

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: 38.09  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1143464692  10 DVLLA--LGNRQVNEIFLAHLPPADsivpPQINEKSARPAREAWIKAKYVERRFA 62
Cdd:cd08848    67 ELLLAknVGNNSFNDIMEGNLPSPS----PKPSPSSDMTARKEYITAKYVEHRFS 117
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 199-269 2.64e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143464692 199 GQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADI 269
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
Ank_4 pfam13637
Ankyrin repeats (many copies);
222-273 2.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1143464692 222 NTPLHLAAKEGHtLPVCQ-LLKRGADSNLANVDSKTPLDIAMECTHADIVTLF 273
Cdd:pfam13637   2 LTALHAAAASGH-LELLRlLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 222-251 2.98e-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. 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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1143464692 222 NTPLHLAA-KEGHTLPVCQLLKRGADSNLAN 251
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ArfGap_AGAP cd08836
ArfGAP with GTPase domain, ANK repeat and PH domains; The AGAP subfamily of ADP-ribosylation ...
 7-57 3.11e-03

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: 36.89  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1143464692   7 ELRDVLLALGNRQVNEIFLAHLPPADSIVPpqineKSARPAREAWIKAKYV 57
Cdd:cd08836    63 ELLKVMSAIGNDLANSVWEGNTQGRTKPTP-----DSSREEKERWIRAKYE 108
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 195-258 3.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 3.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143464692 195 ATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGH-TLPVCQLLKRGADSNLANVDSKTPL 258
Cdd:PHA02876  247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 187-216 3.63e-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 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1143464692  187 NGTTALHIATRNGQTAAVEFLLLNGAKINM 216
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 222-248 4.01e-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: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 4.01e-03
                          10        20
                  ....*....|....*....|....*..
gi 1143464692 222 NTPLHLAAKEGHTLPVCQLLKRGADSN 248
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02741 PHA02741
hypothetical protein; Provisional
 164-274 4.46e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143464692 164 CECGDLLALMTAYAQGFDLNALHN-----GTTALHIA--TRNGQTAA--VEFLLLNGAKIN---MLDEklNTPLHLAA-K 230
Cdd:PHA02741   31 CGCFDIIARFTPFIRGDCHAAALNatddaGQMCIHIAaeKHEAQLAAeiIDHLIELGADINaqeMLEG--DTALHLAAhR 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1143464692 231 EGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLFR 274
Cdd:PHA02741  109 RDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 179-248 4.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143464692 179 GFDLNALHN-GTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSN 248
Cdd:PHA03100  182 GVPINIKDVyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 187-262 7.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 7.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143464692 187 NGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAM 262
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
ArfGap_ADAP cd08832
ArfGap with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) ...
 1-56 9.90e-03

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: 35.31  E-value: 9.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143464692   1 MDSIDNELRDVLLALGNRQVNEIFLAHLP-------PADSIVppqineksarpAREAWIKAKY 56
Cdd:cd08832    62 LDNWDDSQVEFMEENGNEKAKAKYEAHVPafyrrptPTDPQV-----------LREQWIRAKY 113
 
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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