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Conserved domains on  [gi|398366675|ref|NP_010812|]
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GTPase-activating protein AGE1 [Saccharomyces cerevisiae S288C]

Protein Classification

COG5347 family protein( domain architecture ID 11475024)

COG5347 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 164-480 1.17e-92

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: 283.98  E-value: 1.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 164 AGASNRDELLSIVRKIDKSNLKCCDCGSTAtVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLLQN 243
Cdd:COG5347    1 MSTKSEDRKLLKLLKSDSSNKKCADCGAPN-PTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTEEELRRMEVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 244 NVSNSNvnAIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKFVIDSNQGREASLKSLIKAIHLDSVFMMQRAIAQSK 323
Cdd:COG5347   80 GNSNAN--RFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKFIDDSSSPSDFSSFSASSTRTVDSVDDRLDSESQSR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 324 YSLRELTASEKEQNDLNHSSIFQYSLKHYEIVDGTPI---FFITEFLLCNGIHIDNLPKITTNWSPKV-LEYWETKLEMY 399
Cdd:COG5347  158 SSSASLGNSNRPDDELNVESFQSTGSKPRSLTSTKSNkdnLLNSELLTLNSLLSSNSEVGSGTKSRSDaQEKSSTKATES 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 400 GTFQAVNTSRPRSGPHLNMHSNVDS-ASSYNKKHDLRVNIPERSASASKRWSLSSIPKSSQNLMSPTNLLTMHKSLKLAK 478
Cdd:COG5347  238 VKPGPVNTSSTSSLPPAIKRSPVQQlESFTTTPVYFPVNTPATFDATLKSYYSSLTANIAQNGFSPTNADLNDKAQQKKA 317


                 ..
gi 398366675 479 KD 480
Cdd:COG5347  318 WD 319
 
Name Accession Description Interval E-value
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 164-480 1.17e-92

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: 283.98  E-value: 1.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 164 AGASNRDELLSIVRKIDKSNLKCCDCGSTAtVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLLQN 243
Cdd:COG5347    1 MSTKSEDRKLLKLLKSDSSNKKCADCGAPN-PTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTEEELRRMEVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 244 NVSNSNvnAIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKFVIDSNQGREASLKSLIKAIHLDSVFMMQRAIAQSK 323
Cdd:COG5347   80 GNSNAN--RFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKFIDDSSSPSDFSSFSASSTRTVDSVDDRLDSESQSR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 324 YSLRELTASEKEQNDLNHSSIFQYSLKHYEIVDGTPI---FFITEFLLCNGIHIDNLPKITTNWSPKV-LEYWETKLEMY 399
Cdd:COG5347  158 SSSASLGNSNRPDDELNVESFQSTGSKPRSLTSTKSNkdnLLNSELLTLNSLLSSNSEVGSGTKSRSDaQEKSSTKATES 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 400 GTFQAVNTSRPRSGPHLNMHSNVDS-ASSYNKKHDLRVNIPERSASASKRWSLSSIPKSSQNLMSPTNLLTMHKSLKLAK 478
Cdd:COG5347  238 VKPGPVNTSSTSSLPPAIKRSPVQQlESFTTTPVYFPVNTPATFDATLKSYYSSLTANIAQNGFSPTNADLNDKAQQKKA 317


                 ..
gi 398366675 479 KD 480
Cdd:COG5347  318 WD 319
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 173-296 1.12e-37

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: 134.01  E-value: 1.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675   173 LSIVRKIdKSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLlqNNVSNSNVNA 252
Cdd:smart00105   1 LKLLRSI-PGNKKCFDCGA-PNPTWASVNLGVFLCIECSGIHRSLGVHISKVRSLTLDTWTEEELRLL--QKGGNENANS 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 398366675   253 IYESNLRNFPVKKITANsDDSERSKFIIDKYQFKKFVIDSNQGR 296
Cdd:smart00105  77 IWESNLDDFSLKPPDDD-DQQKYESFIAAKYEEKLFVPPESAEE 119
ArfGap cd08204
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 173-283 3.97e-37

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: 131.85  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 173 LSIVRKIDkSNLKCCDCGSTaTVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLQnNVSNSNVNA 252
Cdd:cd08204    1 LEELLKLP-GNKVCADCGAP-DPRWASINLGVFICIRCSGIHRSLGVHISKVRSLTLDSWTP-EQVELMK-AIGNARANA 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 398366675 253 IYESNLRNFPvKKITANSDDSERSKFIIDKY 283
Cdd:cd08204   77 YYEANLPPGF-KKPTPDSSDEEREQFIRAKY 106
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 170-292 5.90e-33

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: 121.18  E-value: 5.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675  170 DELLSIVRKIDkSNLKCCDCGSTAtVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTS--LELMHLLqnnvSN 247
Cdd:pfam01412   1 KRVLRELLKLP-GNKVCADCGAPN-PTWASVNLGIFICIDCSGVHRSLGVHISKVRSLTLDTWTDeqLELMKAG----GN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 398366675  248 SNVNAIYESNLRNFPvkKITANSDDSERSKFIIDKYQFKKFVIDS 292
Cdd:pfam01412  75 DRANEFWEANLPPSY--KPPPSSDREKRESFIRAKYVEKKFAKPG 117
PLN03114 PLN03114
ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
 165-241 2.84e-08

ADP-ribosylation factor GTPase-activating protein AGD10; Provisional


Pssm-ID: 178661 [Multi-domain]  Cd Length: 395  Bit Score: 55.63  E-value: 2.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366675 165 GASNRDELLSIVRKID-KSNLKCC-DCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLL 241
Cdd:PLN03114   2 ASENLNDKISVFKKLKaKSDNKICfDCNAKNPT-WASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSSEQLKMMI 79
 
Name Accession Description Interval E-value
COG5347 COG5347
GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ...
 164-480 1.17e-92

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: 283.98  E-value: 1.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 164 AGASNRDELLSIVRKIDKSNLKCCDCGSTAtVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLLQN 243
Cdd:COG5347    1 MSTKSEDRKLLKLLKSDSSNKKCADCGAPN-PTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTEEELRRMEVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 244 NVSNSNvnAIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKFVIDSNQGREASLKSLIKAIHLDSVFMMQRAIAQSK 323
Cdd:COG5347   80 GNSNAN--RFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKFIDDSSSPSDFSSFSASSTRTVDSVDDRLDSESQSR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 324 YSLRELTASEKEQNDLNHSSIFQYSLKHYEIVDGTPI---FFITEFLLCNGIHIDNLPKITTNWSPKV-LEYWETKLEMY 399
Cdd:COG5347  158 SSSASLGNSNRPDDELNVESFQSTGSKPRSLTSTKSNkdnLLNSELLTLNSLLSSNSEVGSGTKSRSDaQEKSSTKATES 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 400 GTFQAVNTSRPRSGPHLNMHSNVDS-ASSYNKKHDLRVNIPERSASASKRWSLSSIPKSSQNLMSPTNLLTMHKSLKLAK 478
Cdd:COG5347  238 VKPGPVNTSSTSSLPPAIKRSPVQQlESFTTTPVYFPVNTPATFDATLKSYYSSLTANIAQNGFSPTNADLNDKAQQKKA 317


                 ..
gi 398366675 479 KD 480
Cdd:COG5347  318 WD 319
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 173-296 1.12e-37

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: 134.01  E-value: 1.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675   173 LSIVRKIdKSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLlqNNVSNSNVNA 252
Cdd:smart00105   1 LKLLRSI-PGNKKCFDCGA-PNPTWASVNLGVFLCIECSGIHRSLGVHISKVRSLTLDTWTEEELRLL--QKGGNENANS 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 398366675   253 IYESNLRNFPVKKITANsDDSERSKFIIDKYQFKKFVIDSNQGR 296
Cdd:smart00105  77 IWESNLDDFSLKPPDDD-DQQKYESFIAAKYEEKLFVPPESAEE 119
ArfGap cd08204
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 173-283 3.97e-37

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: 131.85  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 173 LSIVRKIDkSNLKCCDCGSTaTVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLQnNVSNSNVNA 252
Cdd:cd08204    1 LEELLKLP-GNKVCADCGAP-DPRWASINLGVFICIRCSGIHRSLGVHISKVRSLTLDSWTP-EQVELMK-AIGNARANA 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 398366675 253 IYESNLRNFPvKKITANSDDSERSKFIIDKY 283
Cdd:cd08204   77 YYEANLPPGF-KKPTPDSSDEEREQFIRAKY 106
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 170-292 5.90e-33

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: 121.18  E-value: 5.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675  170 DELLSIVRKIDkSNLKCCDCGSTAtVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTS--LELMHLLqnnvSN 247
Cdd:pfam01412   1 KRVLRELLKLP-GNKVCADCGAPN-PTWASVNLGIFICIDCSGVHRSLGVHISKVRSLTLDTWTDeqLELMKAG----GN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 398366675  248 SNVNAIYESNLRNFPvkKITANSDDSERSKFIIDKYQFKKFVIDS 292
Cdd:pfam01412  75 DRANEFWEANLPPSY--KPPPSSDREKRESFIRAKYVEKKFAKPG 117
ArfGap_ACAP cd08835
ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins; ArfGAP ...
 183-289 3.84e-31

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: 116.20  E-value: 3.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 183 NLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLqNNVSNSNVNAIYESNLRNFP 262
Cdd:cd08835   13 NAQCCDCGSPDP-RWASINLGVTLCIECSGIHRSLGVHVSKVRSLTLDSWEP-ELLKVM-LELGNDVVNRIYEANVPDDG 89

                         90       100
                 ....*....|....*....|....*..
gi 398366675 263 VKKITANSDDSERSKFIIDKYQFKKFV 289
Cdd:cd08835   90 SVKPTPDSSRQEREAWIRAKYVEKKFV 116
ArfGap_ASAP cd08834
ArfGAP domain of ASAP (Arf GAP, SH3, ANK repeat and PH domains) subfamily of ADP-ribosylation ...
 168-290 4.05e-30

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: 113.47  E-value: 4.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 168 NRDELLSIVRKIdKSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELmhLLQNNVSN 247
Cdd:cd08834    1 LTKSIIAEVKRL-PGNDVCCDCGS-PDPTWLSTNLGILTCIECSGVHRELGVHVSRIQSLTLDNLGTSEL--LLARNLGN 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 398366675 248 SNVNAIYESNLRnfPVKKITANSDDSERSKFIIDKYQFKKFVI 290
Cdd:cd08834   77 EGFNEIMEANLP--PGYKPTPNSDMEERKDFIRAKYVEKKFVV 117
ArfGap_ACAP1 cd08852
ArfGAP domain of ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domains 1); ACAP1 belongs ...
 171-289 2.08e-24

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: 97.72  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 171 ELLSIVRKIDkSNLKCCDCGsTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLqNNVSNSNV 250
Cdd:cd08852    2 HAVAQVQSVD-GNAQCCDCR-EPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEP-ELVKLM-CELGNVII 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398366675 251 NAIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKFV 289
Cdd:cd08852   78 NQIYEARIEAMAIKKPGPSSSRQEKEAWIRAKYVEKKFI 116
ArfGap_ACAP3 cd08850
ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domains 3); ACAP3 belongs ...
 174-289 8.04e-24

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: 96.17  E-value: 8.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 174 SIVRKIDK--SNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLqNNVSNSNVN 251
Cdd:cd08850    2 SILQRVQSiaGNDQCCDCGQPDP-RWASINLGILLCIECSGIHRSLGVHCSKVRSLTLDSWEP-ELLKLM-CELGNSTVN 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366675 252 AIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKFV 289
Cdd:cd08850   79 QIYEAQCEELGLKKPTASSSRQDKEAWIKAKYVEKKFL 116
ArfGap_AGAP cd08836
ArfGAP with GTPase domain, ANK repeat and PH domains; The AGAP subfamily of ADP-ribosylation ...
 176-283 1.41e-22

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: 92.35  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 176 VRKIdKSNLKCCDCGsTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLQnNVSNSNVNAIYE 255
Cdd:cd08836    6 IRNV-RGNDHCVDCG-APNPDWASLNLGALMCIECSGIHRNLGTHISRVRSLDLDDWPV-ELLKVMS-AIGNDLANSVWE 81

                         90       100
                 ....*....|....*....|....*...
gi 398366675 256 SNLRNfpVKKITANSDDSERSKFIIDKY 283
Cdd:cd08836   82 GNTQG--RTKPTPDSSREEKERWIRAKY 107
ArfGap_ACAP2 cd08851
ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domains 2); ACAP2 belongs ...
 183-289 9.01e-22

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: 90.43  E-value: 9.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 183 NLKCCDCGsTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLqNNVSNSNVNAIYESNLRNFP 262
Cdd:cd08851   13 NASCCDCG-LADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEP-ELLKLM-CELGNDVINRIYEARVEKMG 89

                         90       100
                 ....*....|....*....|....*..
gi 398366675 263 VKKITANSDDSERSKFIIDKYQFKKFV 289
Cdd:cd08851   90 AKKPQPGGQRQEKEAYIRAKYVERKFV 116
ArfGap_ARAP cd08837
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing proteins; The ARAP subfamily ...
 181-288 4.78e-20

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: 85.51  E-value: 4.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 181 KSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLD----NFTSLELMHLLQNNVSNSnvnaIYES 256
Cdd:cd08837   11 PANRFCADCGA-PDPDWASINLCVVICKQCAGEHRSLGSNISKVRSLKMDtkvwTEELVELFLKLGNDRANR----FWAA 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398366675 257 NLRnfPVKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd08837   86 NLP--PSEALHPDADSEQRREFITAKYREGKY 115
ArfGap_ASAP1 cd08848
ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein 1); ...
 183-288 8.95e-20

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: 85.09  E-value: 8.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 183 NLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELmhLLQNNVSNSNVNAIYESNLRNfP 262
Cdd:cd08848   15 NEVCCDCGSPDP-TWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSEL--LLAKNVGNNSFNDIMEGNLPS-P 90

                         90       100
                 ....*....|....*....|....*.
gi 398366675 263 VKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd08848   91 SPKPSPSSDMTARKEYITAKYVEHRF 116
ArfGap_ASAP3 cd17900
ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and PH domain-containing protein 3); The ...
 183-289 2.53e-19

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: 83.74  E-value: 2.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 183 NLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELmhLLQNNVSNSNVNAIYESNLRNFP 262
Cdd:cd17900   15 NSQCCDCGA-PDPTWLSTNLGILTCIECSGIHRELGVRYSRIQSLTLDLLSTSEL--LLAVSMGNTRFNEVMEATLPAHG 91

                         90       100
                 ....*....|....*....|....*..
gi 398366675 263 VKKITANSDDSERSKFIIDKYQFKKFV 289
Cdd:cd17900   92 GPKPSAESDMGTRKDYIMAKYVEHRFV 118
ArfGap_ADAP cd08832
ArfGap with dual PH domains; The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) ...
 168-283 5.18e-19

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: 82.31  E-value: 5.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 168 NRDELLSIVRKidKSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLLQnnVSN 247
Cdd:cd08832    4 NKKRLLELLKL--PGNNTCADCGA-PDPEWASYNLGVFICLDCSGIHRSLGTHISKVKSLRLDNWDDSQVEFMEE--NGN 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366675 248 SNVNAIYESNLrnfPV--KKITANSDDSERSKFIIDKY 283
Cdd:cd08832   79 EKAKAKYEAHV---PAfyRRPTPTDPQVLREQWIRAKY 113
ArfGap_SMAP cd08839
Stromal membrane-associated proteins; a subfamily of the ArfGAP family; The SMAP subfamily of ...
 172-283 1.02e-17

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: 78.47  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 172 LLSIVRkiDKSNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLLQnnVSNSNVN 251
Cdd:cd08839    1 LAKLLR--EEDNKYCADCGAKGP-RWASWNLGVFICIRCAGIHRNLGVHISKVKSVNLDSWTPEQVQSMQE--MGNARAN 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 398366675 252 AIYESNL-RNFPVKKitansDDSERSKFIIDKY 283
Cdd:cd08839   76 AYYEANLpDGFRRPQ-----TDSALENFIRDKY 103
ArfGap_ASAP2 cd08849
ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain, ANK repeat and PH domain-containing protein 2) ...
 171-288 1.28e-17

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: 78.86  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 171 ELLSIVRKIDKSNLkCCDCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELmhLLQNNVSNSNV 250
Cdd:cd08849    4 EIISEVQRMTGNDV-CCDCGAPDPT-WLSTNLGILTCIECSGIHRELGVHYSRMQSLTLDVLGTSEL--LLAKNIGNAGF 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366675 251 NAIYESNLRNFPVKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd08849   80 NEIMEACLPAEDVVKPNPGSDMNARKDYITAKYIERRY 117
ArfGap_ArfGap1 cd08830
Arf1 GTPase-activating protein 1; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 176-240 1.55e-17

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: 78.31  E-value: 1.55e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366675 176 VRKIDkSNLKCCDCGsTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFT--SLELMHL 240
Cdd:cd08830    8 LQKLP-GNNRCFDCG-APNPQWASVSYGIFICLECSGVHRGLGVHISFVRSITMDSWSekQLKKMEL 72
ArfGap_GIT cd08833
The GIT subfamily of ADP-ribosylation factor GTPase-activating proteins; The GIT (G-protein ...
 178-283 3.96e-16

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: 74.26  E-value: 3.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 178 KIDKSNLKCC-DCGStATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTS--LELMHLLqnnvSNSNVNAIY 254
Cdd:cd08833    2 RGKSSNARVCaDCSA-PDPEWASINRGVLICDECCSIHRSLGRHISQVKSLRKDQWPPslLEMVQTL----GNNGANSIW 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 398366675 255 ESNL----RNFPVKKITANSDDSERSKFIIDKY 283
Cdd:cd08833   77 EHSLldpsQSGKRKPIPPDPVHPTKEEFIKAKY 109
ArfGap_ArfGap1_like cd08959
ARF1 GTPase-activating protein 1-like; ArfGAP (ADP Ribosylation Factor GTPase Activating ...
 169-237 7.65e-16

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: 73.32  E-value: 7.65e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366675 169 RDELLSIVRKIDKsNLKCCDCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLEL 237
Cdd:cd08959    1 TRAVFKKLRSKPE-NKVCFDCGAKNPQ-WASVTYGIFICLDCSGVHRGLGVHISFVRSTTMDKWTEEQL 67
ArfGap_ARAP2 cd08856
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 2; The ARAP subfamily ...
 180-288 2.75e-15

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: 72.25  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 180 DKSNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLD-NFTSLELMHLLqNNVSNSNVNAIYESNL 258
Cdd:cd08856   15 NESNRSCADCKAPDP-DWASINLCVVICKKCAGQHRSLGPKDSKVRSLKMDaSIWSNELIELF-IVVGNKPANLFWAANL 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 398366675 259 rnFPVKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd08856   93 --FSEEDLHMDSDVEQRTPFITQKYKEGKF 120
ArfGap_ArfGap2_3_like cd08831
Arf1 GTPase-activating protein 2/3-like; ArfGAP (ADP Ribosylation Factor GTPase Activating ...
 169-240 4.39e-15

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: 71.42  E-value: 4.39e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366675 169 RDELLSIVRKIdKSNLKCCDCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLEL--MHL 240
Cdd:cd08831    2 RDAIFKKLRSK-PENKVCFDCGAKNPT-WASVTFGVFLCLDCSGVHRSLGVHISFVRSTNLDSWTPEQLrrMKV 73
ArfGap_AGAP1 cd08854
ArfGAP with GTPase domain, ANK repeat and PH domain 1; The AGAP subfamily of ADP-ribosylation ...
 181-284 8.47e-15

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: 70.42  E-value: 8.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 181 KSNLKCCDCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLqNNVSNSNVNAIYESNLRN 260
Cdd:cd08854   11 KGNSLCVDCGAPNPT-WASLNLGALICIECSGIHRNLGTHLSRVRSLDLDDWPR-ELTLVL-TAIGNHMANSIWESCTQG 87

                         90       100
                 ....*....|....*....|....
gi 398366675 261 fpVKKITANSDDSERSKFIIDKYQ 284
Cdd:cd08854   88 --RTKPAPDSSREERESWIRAKYE 109
ArfGap_ARAP1 cd17901
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 1; The ARAP subfamily ...
 182-288 1.70e-14

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: 69.84  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 182 SNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDN--FTSlELMHLLQNNVSNSNVNaIYESNLR 259
Cdd:cd17901   12 SNRFCADCGSPKP-DWASVNLCVVICKRCAGEHRGLGPSVSKVRSLKMDRkvWTE-ELIELFLLLGNGKANQ-FWAANVP 88

                         90       100
                 ....*....|....*....|....*....
gi 398366675 260 nfPVKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd17901   89 --PSEALCPSSSSEERRHFITAKYKEGKY 115
ArfGap_AGAP3 cd08855
ArfGAP with GTPase domain, ANK repeat and PH domain 3; The AGAP subfamily of ADP-ribosylation ...
 176-284 2.13e-14

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: 69.31  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 176 VRKIdKSNLKCCDCgSTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFtSLELMhLLQNNVSNSNVNAIYE 255
Cdd:cd08855    8 IRNV-RGNSFCIDC-DAPNPDWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDW-PVELS-MVMTAIGNAMANSVWE 83

                         90       100
                 ....*....|....*....|....*....
gi 398366675 256 SNLRNFpvKKITANSDDSERSKFIIDKYQ 284
Cdd:cd08855   84 GALDGY--SKPGPDSTREEKERWIRAKYE 110
ArfGap_AGAP2 cd08853
ArfGAP with GTPase domain, ANK repeat and PH domain 2; The AGAP subfamily of ADP-ribosylation ...
 173-284 1.20e-13

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: 66.96  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 173 LSIVRKIdKSNLKCCDCgSTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFtSLELMHLLQNNVSNSNVNA 252
Cdd:cd08853    4 LQSIRNM-RGNSHCVDC-ETQNPKWASLNLGVLMCIECSGIHRNLGTHLSRVRSLDLDDW-PVELRKVMSSIGNELANSI 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398366675 253 IYESNLRNFpvkKITANSDDSERSKFIIDKYQ 284
Cdd:cd08853   81 WEGSSQGQT---KPSSDSTREEKERWIRAKYE 109
ArfGap_ARAP3 cd17902
ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 3; The ARAP subfamily ...
 180-288 1.00e-12

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: 64.54  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 180 DKSNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDnfTSLELMHLLQNNVSNSNVNAIYESNLR 259
Cdd:cd17902   10 NKANRFCADCHASSP-DWASINLCVVICKQCAGQHRSLGSGISKVQSLKLD--TSVWSNEIVQLFIVLGNDRANRFWAAR 86

                         90       100
                 ....*....|....*....|....*....
gi 398366675 260 NFPVKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:cd17902   87 LPASEALHPDATPEQRREFISRKYREGRF 115
ArfGap_SMAP2 cd08859
Stromal membrane-associated protein 2; a subfamily of the ArfGAP family; The SMAP subfamily of ...
 183-287 1.15e-12

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: 64.24  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 183 NLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSlELMHLLQNNVSNSNVNaIYESNL-RNF 261
Cdd:cd08859   10 NKFCADCQSKGP-RWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQ-EQIQCMQEMGNGKANR-LYEAFLpENF 86

                         90       100
                 ....*....|....*....|....*.
gi 398366675 262 PVKKItansdDSERSKFIIDKYQFKK 287
Cdd:cd08859   87 RRPQT-----DQAVEGFIRDKYEKKK 107
ArfGap_ArfGap2 cd09029
Arf1 GTPase-activating protein 2; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 168-237 6.46e-11

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: 59.69  E-value: 6.46e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366675 168 NRDELLSIVRKIDK--SNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLD-NFTSLEL 237
Cdd:cd09029    2 NKTEIQTLFKRLRAipTNKACFDCGAKNP-SWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDsNWNWFQL 73
ArfGap_ArfGap3 cd09028
Arf1 GTPase-activating protein 3; ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) ...
 168-230 2.29e-09

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: 55.07  E-value: 2.29e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366675 168 NRDELLSIVRKIDK--SNLKCCDCGSTaTVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLD 230
Cdd:cd09028    2 SKQDIAAIFKRLRSvpTNKVCFDCGAK-NPSWASITYGVFLCIDCSGIHRSLGVHLSFIRSTELD 65
ArfGap_ADAP2 cd08844
ADAP2 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs ...
 168-232 7.40e-09

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: 53.62  E-value: 7.40e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366675 168 NRDELLSIVRKidKSNLKCCDCGStATVEWVSINLLCILCIKCSGVHRSLgSHISKIRSLTLDNF 232
Cdd:cd08844    4 NKKRLLELLKL--PGNSVCADCGA-PDPDWASYTLGIFICLNCSGVHRNL-PDISRVKSIRLDFW 64
PLN03114 PLN03114
ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
 165-241 2.84e-08

ADP-ribosylation factor GTPase-activating protein AGD10; Provisional


Pssm-ID: 178661 [Multi-domain]  Cd Length: 395  Bit Score: 55.63  E-value: 2.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366675 165 GASNRDELLSIVRKID-KSNLKCC-DCGSTATVeWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNFTSLELMHLL 241
Cdd:PLN03114   2 ASENLNDKISVFKKLKaKSDNKICfDCNAKNPT-WASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSSEQLKMMI 79
ArfGap_GIT2 cd08847
GIT2 GTPase activating protein for Arf; The GIT (G-protein coupled receptor kinase-interacting ...
 181-227 1.29e-07

GIT2 GTPase activating protein for Arf; 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: 350072 [Multi-domain]  Cd Length: 111  Bit Score: 50.02  E-value: 1.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 398366675 181 KSNLKCCDCgSTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSL 227
Cdd:cd08847    6 RSSEVCADC-STSDPRWASVNRGVLICDECCSVHRSLGRHISQVRHL 51
ArfGap_ADAP1 cd08843
ADAP1 GTPase activating protein for Arf, with dual PH domains; The ADAP subfamily, ArfGAPs ...
 168-283 5.37e-07

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: 48.08  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 168 NRDELLSIVRKidKSNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLgSHISKIRSLTLDNFTSLELMHLlqNNVSN 247
Cdd:cd08843    4 RRRAVLELLQR--PGNARCADCGAPDP-DWASYTLGVFICLSCSGIHRNI-PQVSKVKSVRLDAWEEAQVEFM--ASHGN 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366675 248 SNVNAIYESNLRNFPVKkitANSDDSE--RSKFIIDKY 283
Cdd:cd08843   78 DAARARFESKVPSFYYR---PTPSDCQllREQWIRAKY 112
ArfGap_AGFG cd08838
ArfGAP domain of the AGFG subfamily (ArfGAP domain and FG repeat-containing proteins); The ...
 175-288 1.38e-06

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: 46.80  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 175 IVRKIDKS--NLKCCDCGSTATVeWVSINLLCILCIKCSGVHRSLGsHisKIRSLTLDNFTSLElMHLLQnNVSNSNVNA 252
Cdd:cd08838    3 ILRELLKLpeNKRCFDCGQRGPT-YVNLTFGTFVCTTCSGIHREFN-H--RVKSISMSTFTPEE-VEFLQ-AGGNEVARK 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398366675 253 IY--ESNLRNFPVKKitaNSDDSERSKFIIDKYQFKKF 288
Cdd:cd08838   77 IWlaKWDPRTDPEPD---SGDDQKIREFIRLKYVDKRW 111
ArfGap_GIT1 cd08846
GIT1 GTPase activating protein for Arf; The GIT (G-protein coupled receptor kinase-interacting ...
 177-241 2.18e-05

GIT1 GTPase activating protein for Arf; 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: 350071 [Multi-domain]  Cd Length: 111  Bit Score: 43.55  E-value: 2.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366675 177 RKIDKSNLkCCDCgSTATVEWVSINLLCILCIKCSGVHRSLGSHISKIRSLTLDNF--TSLELMHLL 241
Cdd:cd08846    3 RKGPRAEV-CADC-SAPDPGWASINRGVLICDECCSVHRSLGRHISIVKHLRHSAWppTLLQMVHTL 67
PLN03131 PLN03131
hypothetical protein; Provisional
 169-288 1.27e-04

hypothetical protein; Provisional


Pssm-ID: 178677 [Multi-domain]  Cd Length: 705  Bit Score: 44.77  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 169 RDEllSIVRKIDK--SNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLgSHisKIRSLTLDNFTSLELMHLLQNNVS 246
Cdd:PLN03131   9 RNE--KIIRGLMKlpPNRRCINCNSLGP-QFVCTNFWTFICMTCSGIHREF-TH--RVKSVSMSKFTSQDVEALQNGGNQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 398366675 247 NSNVNAIYESNLRNfpvKKITANSDDSERSKFIIDKYQFKKF 288
Cdd:PLN03131  83 RAREIYLKDWDQQR---QRLPDNSKVDKIREFIKDIYVDKKY 121
PLN03119 PLN03119
putative ADP-ribosylation factor GTPase-activating protein AGD14; Provisional
 175-325 1.90e-03

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


Pssm-ID: 178666  Cd Length: 648  Bit Score: 40.98  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366675 175 IVRKIDK--SNLKCCDCGSTATvEWVSINLLCILCIKCSGVHRSLgSHisKIRSLTLDNFTSLELmHLLQNNVSNSNVNa 252
Cdd:PLN03119  13 IIRGLMKlpPNRRCINCNSLGP-QYVCTTFWTFVCMACSGIHREF-TH--RVKSVSMSKFTSKEV-EVLQNGGNQRARE- 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366675 253 IYESNLrNFPVKKITANSDDSERSKFIIDKYQFKKFVidsnQGREASLKSLIKAIHLDSVFMMQRAIAQSKYS 325
Cdd:PLN03119  87 IYLKNW-DHQRQRLPENSNAERVREFIKNVYVQKKYA----GANDADKPSKDSQDHVSSEDMTRRANSYHSYS 154
 
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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