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Conserved domains on  [gi|25152654|ref|NP_510485|]
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TBC1 domain family member 23 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBC1D23_C-like cd20788
C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains ...
 525-635 1.78e-37

C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains the C-terminal domain of Tre2-Bub2-Cdc16 (TBC) family 23 (TBC1D23), which adopts a Pleckstrin homology (PH) domain fold. It selectively binds to phosphoinositides, in particular, PtdIns(4)P, through one surface while it binds FAM21 via the opposite surface. TBC1D23, which is highly conserved in many eukaryotes but missing in plants and fungi, also possesses an N-terminal domain which is a catalytically inactive TBC domain. TBC1D23 encodes a protein functioning in endosome-to-Golgi trafficking in cells; it is a specificity determinant that links the vesicle to the target membrane. Homozygous mutations of TBC1D23 have been found in patients diagnosed with pontocerebellar hypoplasia (PCH), a group of neurological disorders that affect the brain development, particularly, the pons and cerebellum. Mutation of key residues of TBC1D23 (or FAM21) selectively disrupts the endosomal vesicular trafficking toward the Trans-Golgi Network. This C-terminal domain is missing in some PCH patients.


:

Pssm-ID: 412053  Cd Length: 115  Bit Score: 135.06  E-value: 1.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654 525 EEILLSKEFTETFECQEVFRDG-SINGHIALTRTHIYVLHDVPGKQGYVTTEARHALSTVVAVTSRRSVPEMLTFKLGYE 603
Cdd:cd20788   4 SEWLKKPDVIASFECQEVKENGhMFPSYLLVTETHLYVLREIPDRKGYAKIVVRRPLSSIVKITSKKKHPELITFKYGTS 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 25152654 604 MNGSSKITAVHKLYVPKAGECAKAVKLAIYAL 635
Cdd:cd20788  84 DDDESEITDMDRFYIPKAGDATKAIKQAILKL 115
RabGAP-TBC super family cl46302
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 82-230 2.27e-12

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


The actual alignment was detected with superfamily member pfam00566:

Pssm-ID: 480642  Cd Length: 178  Bit Score: 65.74  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    82 LKNKRSVPELESFLTLYCKKR-------GMDYIkdigwLTILekiLLLNVPAAHEFNVFFAFTTKYIPKDT-RPD----A 149
Cdd:pfam00566  26 FDNGPGQNSLRRILKAYSIYNpdvgycqGMNFI-----AAPL---LLVYLDEEDAFWCFVSLLENYLLRDFyTPDfpglK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   150 QIFDLFRLLLQYHDPQISNHLESLHCSPSMYTKNWFATLFSSSMSTESCHELWKLYIEQGDPFLVFHLAIVFLINAKDEI 229
Cdd:pfam00566  98 RDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLFRVALAILKRFREEL 177


                  .
gi 25152654   230 L 230
Cdd:pfam00566 178 L 178
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 321-421 5.22e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


:

Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 59.78  E-value: 5.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    321 NFFIVDTRSNTDFDSGHFVSSFNLDCVAIVDEPEKFEIALNSlECYKTSRRDEDHYLILGygsDEEDNYMNMLIAMFIQK 400
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFE-ELLKRLGLDKDKPVVVY---CRSGNRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|.
gi 25152654    401 GKLHVSFVQGGYKKLHDCIGQ 421
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
TBC1D23_C-like cd20788
C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains ...
 525-635 1.78e-37

C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains the C-terminal domain of Tre2-Bub2-Cdc16 (TBC) family 23 (TBC1D23), which adopts a Pleckstrin homology (PH) domain fold. It selectively binds to phosphoinositides, in particular, PtdIns(4)P, through one surface while it binds FAM21 via the opposite surface. TBC1D23, which is highly conserved in many eukaryotes but missing in plants and fungi, also possesses an N-terminal domain which is a catalytically inactive TBC domain. TBC1D23 encodes a protein functioning in endosome-to-Golgi trafficking in cells; it is a specificity determinant that links the vesicle to the target membrane. Homozygous mutations of TBC1D23 have been found in patients diagnosed with pontocerebellar hypoplasia (PCH), a group of neurological disorders that affect the brain development, particularly, the pons and cerebellum. Mutation of key residues of TBC1D23 (or FAM21) selectively disrupts the endosomal vesicular trafficking toward the Trans-Golgi Network. This C-terminal domain is missing in some PCH patients.


Pssm-ID: 412053  Cd Length: 115  Bit Score: 135.06  E-value: 1.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654 525 EEILLSKEFTETFECQEVFRDG-SINGHIALTRTHIYVLHDVPGKQGYVTTEARHALSTVVAVTSRRSVPEMLTFKLGYE 603
Cdd:cd20788   4 SEWLKKPDVIASFECQEVKENGhMFPSYLLVTETHLYVLREIPDRKGYAKIVVRRPLSSIVKITSKKKHPELITFKYGTS 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 25152654 604 MNGSSKITAVHKLYVPKAGECAKAVKLAIYAL 635
Cdd:cd20788  84 DDDESEITDMDRFYIPKAGDATKAIKQAILKL 115
TBC1D23_C pfam19430
TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a ...
 453-615 1.00e-18

TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a family of TBC domain-containing Rab-specific GTPase-activating proteins, which plays a role in endosome-to-Golgi trafficking. It acts as a bridging factor in which the TBC domain binds to Golgi adaptor proteins golgin-97 and golgin-245 and its C-terminal to FAM21 subunit of the WASH complex, which regulates multiple endosomal trafficking routes. TBC1D23 is important for normal brain development, especially in axonal and dendritic growth. This entry represents the C-terminal domain that contains residues for specific FAM21 binding and for the cargo of endosome-derived carriers. It adopts a fold similar to the Pleckstrin homology (PH) domain. Mutations in this protein, and particularly in this domain, are linked with Pontocerebellar hypoplasia (PCH), suggesting that the TBC1D23 C-terminal domain is required for neuronal growth and brain development.


Pssm-ID: 437262  Cd Length: 225  Bit Score: 85.60  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   453 KMKSAVSNTSSRMKERVEAVVFPigeEKKLDDKHADSKQRHGKRYRQ-QSVFTI---DENSDDEMAAGAAVDENPKEEIL 528
Cdd:pfam19430  54 KVISFIENTSTPVDRMSFNLPWP---DRSCTERHVSSSDRVGKPYRGvKPVFSIgdeEEYDTDEIDSSSMSDDDRKEVVN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   529 LSK-----EFTETFECQEVFRDGSI-NGHIALTRTHIYVLHDVPGKQGYVTTEARHALSTVVAVTSRRSVPEMLTFKLGY 602
Cdd:pfam19430 131 IQTwinkpDVKHHFPCKEVKESGHMfPSHLLVTATHMYCLREIASRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGN 210

                         170
                  ....*....|...
gi 25152654   603 EMNGSSKITAVHK 615
Cdd:pfam19430 211 SSASGIEILAIER 223
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 82-230 2.27e-12

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 65.74  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    82 LKNKRSVPELESFLTLYCKKR-------GMDYIkdigwLTILekiLLLNVPAAHEFNVFFAFTTKYIPKDT-RPD----A 149
Cdd:pfam00566  26 FDNGPGQNSLRRILKAYSIYNpdvgycqGMNFI-----AAPL---LLVYLDEEDAFWCFVSLLENYLLRDFyTPDfpglK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   150 QIFDLFRLLLQYHDPQISNHLESLHCSPSMYTKNWFATLFSSSMSTESCHELWKLYIEQGDPFLVFHLAIVFLINAKDEI 229
Cdd:pfam00566  98 RDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLFRVALAILKRFREEL 177


                  .
gi 25152654   230 L 230
Cdd:pfam00566 178 L 178
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 43-230 3.53e-12

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 66.18  E-value: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654     43 WMRLLGVsmKPNPLDDWDQLY-NLNNQCALRNDCRKLANGLKNKRSVPELESF--------------LTLYCKKR-GMDY 106
Cdd:smart00164  14 WKLLLNA--QPMDTSADKDLYsRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFqdkegpgqeslrrvLKAYALYNpEVGY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    107 IKDIGWLTILekiLLLNVPAAHE-FNVFFAFTTKYIPKDTRPDAQIFDL----FRLLLQYHDPQISNHLESLHCSPSMYT 181
Cdd:smart00164  92 CQGMNFLAAP---LLLVMEDEEDaFWCLVKLMERYGPNFYLPDMSGLQLdllqLDRLVKEYDPDLYKHLKDLGITPSLYA 168

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 25152654    182 KNWFATLFSSSMSTESCHELWKLYIEQGDPFLvFHLAIVFLINAKDEIL 230
Cdd:smart00164 169 LRWFLTLFARELPLEIVLRIWDVLFAEGSDFL-FRVALALLKLHRDVLL 216
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 321-421 5.22e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 59.78  E-value: 5.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    321 NFFIVDTRSNTDFDSGHFVSSFNLDCVAIVDEPEKFEIALNSlECYKTSRRDEDHYLILGygsDEEDNYMNMLIAMFIQK 400
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFE-ELLKRLGLDKDKPVVVY---CRSGNRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|.
gi 25152654    401 GKLHVSFVQGGYKKLHDCIGQ 421
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAAGPP 100
COG5210 COG5210
GTPase-activating protein [General function prediction only];
152-236 5.14e-04

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 42.87  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654 152 FDLFRLLLQYHDPQISNHLESLHCSPSMYTKNWFATLFSSSMSTESCHELWKLYIEQGDPFLvFHLAIVFLINAKDEILQ 231
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSML-FQLALAILKLLRDKLLK 428


                ....*
gi 25152654 232 VKRDE 236
Cdd:COG5210 429 LDSDE 433
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 324-414 7.74e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 36.31  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   324 IVDTRSNTDFDSGHFVSSFNLDCVAIVDEPEKFEIALNSLEcyktSRRDEDHYLILGYGSDEEDNYMNMLIAMfiqkGKL 403
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLL----ELLKDKPIVVYCNSGNRAAAAAALLKAL----GYK 79

                          90
                  ....*....|.
gi 25152654   404 HVSFVQGGYKK 414
Cdd:pfam00581  80 NVYVLDGGFEA 90
 
Name Accession Description Interval E-value
TBC1D23_C-like cd20788
C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains ...
 525-635 1.78e-37

C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains the C-terminal domain of Tre2-Bub2-Cdc16 (TBC) family 23 (TBC1D23), which adopts a Pleckstrin homology (PH) domain fold. It selectively binds to phosphoinositides, in particular, PtdIns(4)P, through one surface while it binds FAM21 via the opposite surface. TBC1D23, which is highly conserved in many eukaryotes but missing in plants and fungi, also possesses an N-terminal domain which is a catalytically inactive TBC domain. TBC1D23 encodes a protein functioning in endosome-to-Golgi trafficking in cells; it is a specificity determinant that links the vesicle to the target membrane. Homozygous mutations of TBC1D23 have been found in patients diagnosed with pontocerebellar hypoplasia (PCH), a group of neurological disorders that affect the brain development, particularly, the pons and cerebellum. Mutation of key residues of TBC1D23 (or FAM21) selectively disrupts the endosomal vesicular trafficking toward the Trans-Golgi Network. This C-terminal domain is missing in some PCH patients.


Pssm-ID: 412053  Cd Length: 115  Bit Score: 135.06  E-value: 1.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654 525 EEILLSKEFTETFECQEVFRDG-SINGHIALTRTHIYVLHDVPGKQGYVTTEARHALSTVVAVTSRRSVPEMLTFKLGYE 603
Cdd:cd20788   4 SEWLKKPDVIASFECQEVKENGhMFPSYLLVTETHLYVLREIPDRKGYAKIVVRRPLSSIVKITSKKKHPELITFKYGTS 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 25152654 604 MNGSSKITAVHKLYVPKAGECAKAVKLAIYAL 635
Cdd:cd20788  84 DDDESEITDMDRFYIPKAGDATKAIKQAILKL 115
TBC1D23_C pfam19430
TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a ...
 453-615 1.00e-18

TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a family of TBC domain-containing Rab-specific GTPase-activating proteins, which plays a role in endosome-to-Golgi trafficking. It acts as a bridging factor in which the TBC domain binds to Golgi adaptor proteins golgin-97 and golgin-245 and its C-terminal to FAM21 subunit of the WASH complex, which regulates multiple endosomal trafficking routes. TBC1D23 is important for normal brain development, especially in axonal and dendritic growth. This entry represents the C-terminal domain that contains residues for specific FAM21 binding and for the cargo of endosome-derived carriers. It adopts a fold similar to the Pleckstrin homology (PH) domain. Mutations in this protein, and particularly in this domain, are linked with Pontocerebellar hypoplasia (PCH), suggesting that the TBC1D23 C-terminal domain is required for neuronal growth and brain development.


Pssm-ID: 437262  Cd Length: 225  Bit Score: 85.60  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   453 KMKSAVSNTSSRMKERVEAVVFPigeEKKLDDKHADSKQRHGKRYRQ-QSVFTI---DENSDDEMAAGAAVDENPKEEIL 528
Cdd:pfam19430  54 KVISFIENTSTPVDRMSFNLPWP---DRSCTERHVSSSDRVGKPYRGvKPVFSIgdeEEYDTDEIDSSSMSDDDRKEVVN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   529 LSK-----EFTETFECQEVFRDGSI-NGHIALTRTHIYVLHDVPGKQGYVTTEARHALSTVVAVTSRRSVPEMLTFKLGY 602
Cdd:pfam19430 131 IQTwinkpDVKHHFPCKEVKESGHMfPSHLLVTATHMYCLREIASRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGN 210

                         170
                  ....*....|...
gi 25152654   603 EMNGSSKITAVHK 615
Cdd:pfam19430 211 SSASGIEILAIER 223
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 82-230 2.27e-12

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 65.74  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    82 LKNKRSVPELESFLTLYCKKR-------GMDYIkdigwLTILekiLLLNVPAAHEFNVFFAFTTKYIPKDT-RPD----A 149
Cdd:pfam00566  26 FDNGPGQNSLRRILKAYSIYNpdvgycqGMNFI-----AAPL---LLVYLDEEDAFWCFVSLLENYLLRDFyTPDfpglK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   150 QIFDLFRLLLQYHDPQISNHLESLHCSPSMYTKNWFATLFSSSMSTESCHELWKLYIEQGDPFLVFHLAIVFLINAKDEI 229
Cdd:pfam00566  98 RDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLFRVALAILKRFREEL 177


                  .
gi 25152654   230 L 230
Cdd:pfam00566 178 L 178
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 43-230 3.53e-12

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 66.18  E-value: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654     43 WMRLLGVsmKPNPLDDWDQLY-NLNNQCALRNDCRKLANGLKNKRSVPELESF--------------LTLYCKKR-GMDY 106
Cdd:smart00164  14 WKLLLNA--QPMDTSADKDLYsRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFqdkegpgqeslrrvLKAYALYNpEVGY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    107 IKDIGWLTILekiLLLNVPAAHE-FNVFFAFTTKYIPKDTRPDAQIFDL----FRLLLQYHDPQISNHLESLHCSPSMYT 181
Cdd:smart00164  92 CQGMNFLAAP---LLLVMEDEEDaFWCLVKLMERYGPNFYLPDMSGLQLdllqLDRLVKEYDPDLYKHLKDLGITPSLYA 168

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 25152654    182 KNWFATLFSSSMSTESCHELWKLYIEQGDPFLvFHLAIVFLINAKDEIL 230
Cdd:smart00164 169 LRWFLTLFARELPLEIVLRIWDVLFAEGSDFL-FRVALALLKLHRDVLL 216
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 321-421 5.22e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 59.78  E-value: 5.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654    321 NFFIVDTRSNTDFDSGHFVSSFNLDCVAIVDEPEKFEIALNSlECYKTSRRDEDHYLILGygsDEEDNYMNMLIAMFIQK 400
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFE-ELLKRLGLDKDKPVVVY---CRSGNRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|.
gi 25152654    401 GKLHVSFVQGGYKKLHDCIGQ 421
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAAGPP 100
COG5210 COG5210
GTPase-activating protein [General function prediction only];
152-236 5.14e-04

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 42.87  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654 152 FDLFRLLLQYHDPQISNHLESLHCSPSMYTKNWFATLFSSSMSTESCHELWKLYIEQGDPFLvFHLAIVFLINAKDEILQ 231
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSML-FQLALAILKLLRDKLLK 428


                ....*
gi 25152654 232 VKRDE 236
Cdd:COG5210 429 LDSDE 433
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 324-414 7.74e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 36.31  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152654   324 IVDTRSNTDFDSGHFVSSFNLDCVAIVDEPEKFEIALNSLEcyktSRRDEDHYLILGYGSDEEDNYMNMLIAMfiqkGKL 403
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLL----ELLKDKPIVVYCNSGNRAAAAAALLKAL----GYK 79

                          90
                  ....*....|.
gi 25152654   404 HVSFVQGGYKK 414
Cdd:pfam00581  80 NVYVLDGGFEA 90
 
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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