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Conserved domains on  [gi|1622842648|ref|XP_015008235|]
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ARF GTPase-activating protein GIT2 isoform X14 [Macaca mulatta]

Protein Classification

ARF GTPase-activating protein GIT( domain architecture ID 13213119)

ARF GTPase-activating protein GIT (G protein-coupled receptor kinase-interacting) is a signaling integrator with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GIT1_C pfam12205
G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in ...
 549-662 1.99e-42

G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. The family is found in association with pfam01412, pfam00023, pfam08518. GIT1 plays an important role in cell adhesion, motility, cytoskeletal remodelling and membrane trafficking. To perform this function, it localizes p21-activated kinase (PAK) and PAK-interactive exchange factor to focal adhesions. Its activation is regulated by interaction between its paxillin-binding C terminal and the LD motifs of paxillin. The C terminal folds into a four helix bundle.


:

Pssm-ID: 463492  Cd Length: 110  Bit Score: 148.97  E-value: 1.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648 549 EDVIRKTEQITKNIQELLRAAQENKHDSYIPCSERIHVAVTEMAALFPKKPKSDMVRTSLRLLTSSAYRLQSECKKTLPg 628
Cdd:pfam12205   2 DNVVRQTELITKAIQELLKAAQEGRHSEFLDCAERIRSAVTEMAALFPKSPRSETVREALKALTDAADKLQAECVSLKA- 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622842648 629 DPGSPtdvqLVTQQVIQCAYDIAKAAKQLVTITT 662
Cdd:pfam12205  81 SPGPD----DSSQEIITAAYDIAKAAKELVTLFE 110
ArfGap super family cl28907
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 1-49 3.85e-31

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 cd08847:

Pssm-ID: 355783 [Multi-domain]  Cd Length: 111  Bit Score: 117.43  E-value: 3.85e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASIMSGRRKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08847    63 MVQTLYNNGANSIWEHSLLDPASIMSGKRKANPQDKVHPNKAEFIRAKY 111
GIT_CC pfam16559
GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of ...
 352-416 1.46e-27

GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of GIT (G protein-coupled receptor kinase-interacting) proteins. This coiled-coil region is the surface that associates with the equivalent binding-region on beta-PIX, or p21-activated kinase-interacting exchange factor proteins. Both GIT and PIX complex together to form a scaffold for the formation of multi-protein assemblies. On its own the GIT-CC region assembles into a parallel two-stranded CC in the asymmetric unit. Similarly the PIX coiled-coil region assembles into a trimer. At least in vitro the two regions associate together into a stable heteropentameric complex that consists of one PIX trimer and one GIT dimer.


:

Pssm-ID: 465174  Cd Length: 66  Bit Score: 105.62  E-value: 1.46e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622842648 352 KSLDS-DLSDGPVTVQEFMEVKNALVASEAKIQQLMKVNNNLSDELRIMQKKLQTLQSENSNLRKQ 416
Cdd:pfam16559   1 KSLDSsDLSDGPVTVQEYLELKEALAASEAKIQQLMKVNTNLSDELRLLQSKVQTLQQENADLRDQ 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-208 2.29e-14

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  61 RDDDSVTAkdlskqLHSSVRTGNLETCLRLLSLGAQANFFHPEkGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKT 140
Cdd:COG0666   149 QDNDGNTP------LHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622842648 141 PVDYARQGGHHELAERLVEIQYELTDRLAFYLCGRKPDHKNGQHFIIPQMADSSLDLSELAKAAKKKL 208
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 204-232 8.33e-11

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


:

Pssm-ID: 462506  Cd Length: 29  Bit Score: 57.02  E-value: 8.33e-11
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 204 AKKKLQSLSNHLFEELAMDVYDEVDRRET 232
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 268-296 2.61e-08

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


:

Pssm-ID: 462506  Cd Length: 29  Bit Score: 49.70  E-value: 2.61e-08
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 268 GRQKLARFNAHEFATLVIDILSDAKRRQQ 296
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
 
Name Accession Description Interval E-value
GIT1_C pfam12205
G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in ...
 549-662 1.99e-42

G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. The family is found in association with pfam01412, pfam00023, pfam08518. GIT1 plays an important role in cell adhesion, motility, cytoskeletal remodelling and membrane trafficking. To perform this function, it localizes p21-activated kinase (PAK) and PAK-interactive exchange factor to focal adhesions. Its activation is regulated by interaction between its paxillin-binding C terminal and the LD motifs of paxillin. The C terminal folds into a four helix bundle.


Pssm-ID: 463492  Cd Length: 110  Bit Score: 148.97  E-value: 1.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648 549 EDVIRKTEQITKNIQELLRAAQENKHDSYIPCSERIHVAVTEMAALFPKKPKSDMVRTSLRLLTSSAYRLQSECKKTLPg 628
Cdd:pfam12205   2 DNVVRQTELITKAIQELLKAAQEGRHSEFLDCAERIRSAVTEMAALFPKSPRSETVREALKALTDAADKLQAECVSLKA- 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622842648 629 DPGSPtdvqLVTQQVIQCAYDIAKAAKQLVTITT 662
Cdd:pfam12205  81 SPGPD----DSSQEIITAAYDIAKAAKELVTLFE 110
ArfGap_GIT2 cd08847
GIT2 GTPase activating protein for Arf; The GIT (G-protein coupled receptor kinase-interacting ...
 1-49 3.85e-31

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: 117.43  E-value: 3.85e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASIMSGRRKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08847    63 MVQTLYNNGANSIWEHSLLDPASIMSGKRKANPQDKVHPNKAEFIRAKY 111
GIT_CC pfam16559
GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of ...
 352-416 1.46e-27

GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of GIT (G protein-coupled receptor kinase-interacting) proteins. This coiled-coil region is the surface that associates with the equivalent binding-region on beta-PIX, or p21-activated kinase-interacting exchange factor proteins. Both GIT and PIX complex together to form a scaffold for the formation of multi-protein assemblies. On its own the GIT-CC region assembles into a parallel two-stranded CC in the asymmetric unit. Similarly the PIX coiled-coil region assembles into a trimer. At least in vitro the two regions associate together into a stable heteropentameric complex that consists of one PIX trimer and one GIT dimer.


Pssm-ID: 465174  Cd Length: 66  Bit Score: 105.62  E-value: 1.46e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622842648 352 KSLDS-DLSDGPVTVQEFMEVKNALVASEAKIQQLMKVNNNLSDELRIMQKKLQTLQSENSNLRKQ 416
Cdd:pfam16559   1 KSLDSsDLSDGPVTVQEYLELKEALAASEAKIQQLMKVNTNLSDELRLLQSKVQTLQQENADLRDQ 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-208 2.29e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  61 RDDDSVTAkdlskqLHSSVRTGNLETCLRLLSLGAQANFFHPEkGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKT 140
Cdd:COG0666   149 QDNDGNTP------LHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622842648 141 PVDYARQGGHHELAERLVEIQYELTDRLAFYLCGRKPDHKNGQHFIIPQMADSSLDLSELAKAAKKKL 208
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 1-62 1.99e-11

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: 61.59  E-value: 1.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622842648    1 MVETLYNNGANSIWEHSLLDPASIMsgrrkanPQDKVHPNKAEFIRAKYQMLAFVHRLPCRD 62
Cdd:smart00105  65 LLQKGGNENANSIWESNLDDFSLKP-------PDDDDQQKYESFIAAKYEEKLFVPPESAEE 119
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 204-232 8.33e-11

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 57.02  E-value: 8.33e-11
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 204 AKKKLQSLSNHLFEELAMDVYDEVDRRET 232
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 1.33e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  75 LHSSVRTGNLETCLRLLSLGAQANFFHPEkGNTPLHVASKAGQILQAELLAVYGAdpGTQDSSGKTPVDYARQGGHHELA 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1622842648 155 ERLVEIQYELTDR 167
Cdd:pfam12796  78 KLLLEKGADINVK 90
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 268-296 2.61e-08

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 49.70  E-value: 2.61e-08
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 268 GRQKLARFNAHEFATLVIDILSDAKRRQQ 296
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 204-234 4.35e-07

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 46.39  E-value: 4.35e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622842648  204 AKKKLQSLSNHLFEELAMDVYDEVDRRETDA 234
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 56-157 8.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  56 HRLPCRDD-DSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANF--FHpekGNTPLHVASKAGQILQAELLAVYGADPG 132
Cdd:PTZ00322   66 HNLTTEEViDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCrdYD---GRTPLHIACANGHVQVVRVLLEFGADPT 142

                          90       100
                  ....*....|....*....|....*
gi 1622842648 133 TQDSSGKTPVDYARQGGHHELAERL 157
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLL 167
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 268-298 1.38e-04

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 39.45  E-value: 1.38e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622842648  268 GRQKLARFNAHEFATLVIDILSDAKRRQQGS 298
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 1-57 1.04e-03

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: 39.13  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASImsgrrkanPQDKVHPNKAEFIRAKYQMLAFVHR 57
Cdd:pfam01412  68 LMKAGGNDRANEFWEANLPPSYKP--------PPSSDREKRESFIRAKYVEKKFAKP 116
 
Name Accession Description Interval E-value
GIT1_C pfam12205
G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in ...
 549-662 1.99e-42

G protein-coupled receptor kinase-interacting protein 1 C term; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. The family is found in association with pfam01412, pfam00023, pfam08518. GIT1 plays an important role in cell adhesion, motility, cytoskeletal remodelling and membrane trafficking. To perform this function, it localizes p21-activated kinase (PAK) and PAK-interactive exchange factor to focal adhesions. Its activation is regulated by interaction between its paxillin-binding C terminal and the LD motifs of paxillin. The C terminal folds into a four helix bundle.


Pssm-ID: 463492  Cd Length: 110  Bit Score: 148.97  E-value: 1.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648 549 EDVIRKTEQITKNIQELLRAAQENKHDSYIPCSERIHVAVTEMAALFPKKPKSDMVRTSLRLLTSSAYRLQSECKKTLPg 628
Cdd:pfam12205   2 DNVVRQTELITKAIQELLKAAQEGRHSEFLDCAERIRSAVTEMAALFPKSPRSETVREALKALTDAADKLQAECVSLKA- 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622842648 629 DPGSPtdvqLVTQQVIQCAYDIAKAAKQLVTITT 662
Cdd:pfam12205  81 SPGPD----DSSQEIITAAYDIAKAAKELVTLFE 110
ArfGap_GIT2 cd08847
GIT2 GTPase activating protein for Arf; The GIT (G-protein coupled receptor kinase-interacting ...
 1-49 3.85e-31

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: 117.43  E-value: 3.85e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASIMSGRRKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08847    63 MVQTLYNNGANSIWEHSLLDPASIMSGKRKANPQDKVHPNKAEFIRAKY 111
GIT_CC pfam16559
GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of ...
 352-416 1.46e-27

GIT coiled-coil Rho guanine nucleotide exchange factor; GIT-CC is the coiled-coil region of GIT (G protein-coupled receptor kinase-interacting) proteins. This coiled-coil region is the surface that associates with the equivalent binding-region on beta-PIX, or p21-activated kinase-interacting exchange factor proteins. Both GIT and PIX complex together to form a scaffold for the formation of multi-protein assemblies. On its own the GIT-CC region assembles into a parallel two-stranded CC in the asymmetric unit. Similarly the PIX coiled-coil region assembles into a trimer. At least in vitro the two regions associate together into a stable heteropentameric complex that consists of one PIX trimer and one GIT dimer.


Pssm-ID: 465174  Cd Length: 66  Bit Score: 105.62  E-value: 1.46e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622842648 352 KSLDS-DLSDGPVTVQEFMEVKNALVASEAKIQQLMKVNNNLSDELRIMQKKLQTLQSENSNLRKQ 416
Cdd:pfam16559   1 KSLDSsDLSDGPVTVQEYLELKEALAASEAKIQQLMKVNTNLSDELRLLQSKVQTLQQENADLRDQ 66
ArfGap_GIT1 cd08846
GIT1 GTPase activating protein for Arf; The GIT (G-protein coupled receptor kinase-interacting ...
 1-49 3.13e-22

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: 92.09  E-value: 3.13e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASIMSGRRKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08846    63 MVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPTKSEFIRAKY 111
ArfGap_GIT cd08833
The GIT subfamily of ADP-ribosylation factor GTPase-activating proteins; The GIT (G-protein ...
 1-49 7.45e-22

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: 90.82  E-value: 7.45e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPAsiMSGRRKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08833    63 MVQTLGNNGANSIWEHSLLDPS--QSGKRKPIPPDPVHPTKEEFIKAKY 109
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-208 2.29e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  61 RDDDSVTAkdlskqLHSSVRTGNLETCLRLLSLGAQANFFHPEkGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKT 140
Cdd:COG0666   149 QDNDGNTP------LHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622842648 141 PVDYARQGGHHELAERLVEIQYELTDRLAFYLCGRKPDHKNGQHFIIPQMADSSLDLSELAKAAKKKL 208
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-159 9.70e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 9.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  62 DDDSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHpEKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTP 141
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156

                          90
                  ....*....|....*...
gi 1622842648 142 VDYARQGGHHELAERLVE 159
Cdd:COG0666   157 LHLAAANGNLEIVKLLLE 174
ArfGap smart00105
Putative GTP-ase activating proteins for the small GTPase, ARF; Putative zinc fingers with ...
 1-62 1.99e-11

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: 61.59  E-value: 1.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622842648    1 MVETLYNNGANSIWEHSLLDPASIMsgrrkanPQDKVHPNKAEFIRAKYQMLAFVHRLPCRD 62
Cdd:smart00105  65 LLQKGGNENANSIWESNLDDFSLKP-------PDDDDQQKYESFIAAKYEEKLFVPPESAEE 119
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 204-232 8.33e-11

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 57.02  E-value: 8.33e-11
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 204 AKKKLQSLSNHLFEELAMDVYDEVDRRET 232
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-159 9.47e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 9.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  30 KANPQDKVHPNKAEFIRAKYQMLAFVHRLPCRDDDSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGNTPL 109
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622842648 110 HVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYARQGGHHELAERLVE 159
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 1.33e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  75 LHSSVRTGNLETCLRLLSLGAQANFFHPEkGNTPLHVASKAGQILQAELLAVYGAdpGTQDSSGKTPVDYARQGGHHELA 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1622842648 155 ERLVEIQYELTDR 167
Cdd:pfam12796  78 KLLLEKGADINVK 90
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 268-296 2.61e-08

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 49.70  E-value: 2.61e-08
                          10        20
                  ....*....|....*....|....*....
gi 1622842648 268 GRQKLARFNAHEFATLVIDILSDAKRRQQ 296
Cdd:pfam08518   1 ARQKLARLSNQQFEELVTDVYDELDRRQT 29
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 204-234 4.35e-07

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 46.39  E-value: 4.35e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622842648  204 AKKKLQSLSNHLFEELAMDVYDEVDRRETDA 234
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 56-157 8.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  56 HRLPCRDD-DSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANF--FHpekGNTPLHVASKAGQILQAELLAVYGADPG 132
Cdd:PTZ00322   66 HNLTTEEViDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCrdYD---GRTPLHIACANGHVQVVRVLLEFGADPT 142

                          90       100
                  ....*....|....*....|....*
gi 1622842648 133 TQDSSGKTPVDYARQGGHHELAERL 157
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-145 1.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622842648 103 EKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYA 145
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-135 1.80e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  47 AKYQMLAFVHRL-------PCRDDDSVTAkdlskqLHSSVRTGNLETCLRLLSlgaQANFFHPEKGNTPLHVASKAGQIL 119
Cdd:pfam12796   5 AKNGNLELVKLLlengadaNLQDKNGRTA------LHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1622842648 120 QAELLAVYGADPGTQD 135
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-158 5.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 5.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622842648 105 GNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYARQGGHHELAERLV 158
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 66-159 1.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  66 VTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYA 145
Cdd:PHA02875   63 VKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                          90
                  ....*....|....
gi 1622842648 146 RQGGHHELAERLVE 159
Cdd:PHA02875  143 VMMGDIKGIELLID 156
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 268-298 1.38e-04

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 39.45  E-value: 1.38e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622842648  268 GRQKLARFNAHEFATLVIDILSDAKRRQQGS 298
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
ArfGap cd08204
GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs); ArfGAPs are a family ...
 1-49 4.72e-04

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: 40.17  E-value: 4.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPAsimsgrrKANPQDKVHPNKAEFIRAKY 49
Cdd:cd08204    65 LMKAIGNARANAYYEANLPPGF-------KKPTPDSSDEEREQFIRAKY 106
ArfGap pfam01412
Putative GTPase activating protein for Arf; Putative zinc fingers with GTPase activating ...
 1-57 1.04e-03

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: 39.13  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622842648   1 MVETLYNNGANSIWEHSLLDPASImsgrrkanPQDKVHPNKAEFIRAKYQMLAFVHR 57
Cdd:pfam01412  68 LMKAGGNDRANEFWEANLPPSYKP--------PPSSDREKRESFIRAKYVEKKFAKP 116
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 58-159 1.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  58 LPCRDDDSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFfHPEKGNTPLHVASKAGQILQAELLAVYGADPGTQDSS 137
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90       100
                  ....*....|....*....|..
gi 1622842648 138 GKTPVDYARQGGHHELAERLVE 159
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLID 211
PHA02946 PHA02946
ankyin-like protein; Provisional
 103-162 2.43e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 2.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622842648 103 EKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVdYARQGGHHELAERL-VEIQY 162
Cdd:PHA02946   70 DDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL-YYLSGTDDEVIERInLLVQY 129
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 90-179 3.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  90 LLSLGAQANFFHPEKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYARQGGHHELAERLVEiQYELTDrlA 169
Cdd:PHA02878  153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTD--A 229

                          90
                  ....*....|
gi 1622842648 170 FYLCGRKPDH 179
Cdd:PHA02878  230 RDKCGNTPLH 239
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-187 4.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842648  75 LHSSV-RTGNLETCLRLLSLGAQANFFHPEKGNTPLHVASKAGQILQaeLLAVYGADPGTQDSSGKTPVDYArqgghhel 153
Cdd:PHA02878  238 LHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA-------- 307

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622842648 154 aeRLVEIQYELTDRLAFYLCGRK---PDHKNGQHFII 187
Cdd:PHA02878  308 --VKQYLCINIGRILISNICLLKrikPDIKNSEGFID 342
Ank_4 pfam13637
Ankyrin repeats (many copies);
75-124 9.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 9.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622842648  75 LHSSVRTGNLETCLRLLSLGAQANFFhPEKGNTPLHVASKAGQILQAELL 124
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLL 53
 
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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