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Conserved domains on  [gi|528482482|ref|XP_005165998|]
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TBC1 domain family member 23 isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBC1D23_C pfam19430
TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a ...
 447-670 6.17e-142

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: 413.79  E-value: 6.17e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  447 NVYVHWIVSTSGSHSSLSSADGE-LNSTDGKGVKSLVNKMTFALKSKSVNVKEKVISFIENTSTPVERMSFNLPWPDKGI 525
Cdd:pfam19430   1 NGYGHWIASTSGSRSSINSVDGEsLNGSGDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  526 LERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSISDDDRKEIVNIQTWINKPDVKHHIPCNEVKETGHMFPSHL 605
Cdd:pfam19430  81 TERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482482  606 LITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKFGNNNAAGVEIVAVERYL 670
Cdd:pfam19430 161 LVTATHMYCLREIASRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYL 225
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 98-242 1.71e-16

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: 77.68  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   98 DLVSDVESVITFYCKSR-NVTFTPDLSwpHILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKGRP-----FHLFRLLL 171
Cdd:pfam00566  30 PGQNSLRRILKAYSIYNpDVGYCQGMN--FIAAPLLLVYLDEEDAFWCFVSLLENYLLRDFYTPDFPglkrdLYVFEELL 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528482482  172 QYHEPEFCSFLDTKKITPDSYAINWLGSLFsSHCLP-EVTQALWDVYLQQADPFLIFFLMLIILVNAKDNIL 242
Cdd:pfam00566 108 KKKLPKLYKHLKELGLDPDLFASQWFLTLF-AREFPlSTVLRIWDYFFLEGEKFVLFRVALAILKRFREELL 178
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 324-435 2.35e-06

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. 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 certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member cd01446:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 324 ANQLQPEGVRFFVVDCRPAEQYNAGHLSTAFHLD-SDLMLHNPSEFALSVKSLL--EAQKQSLESGSVAS----GEHLCF 396
Cdd:cd01446    8 AALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCcPTILRRRLQGGKILLQQLLscPEDRDRLRRGESLAvvvyDESSSD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528482482 397 MGSGReeEDMYMNMVLAHFLQKNKEF--VSIAKGGFMALQQ 435
Cdd:cd01446   88 RERLR--EDSTAESVLGKLLRKLQEGcsVYLLKGGFEQFSS 126
 
Name Accession Description Interval E-value
TBC1D23_C pfam19430
TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a ...
 447-670 6.17e-142

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: 413.79  E-value: 6.17e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  447 NVYVHWIVSTSGSHSSLSSADGE-LNSTDGKGVKSLVNKMTFALKSKSVNVKEKVISFIENTSTPVERMSFNLPWPDKGI 525
Cdd:pfam19430   1 NGYGHWIASTSGSRSSINSVDGEsLNGSGDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  526 LERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSISDDDRKEIVNIQTWINKPDVKHHIPCNEVKETGHMFPSHL 605
Cdd:pfam19430  81 TERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482482  606 LITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKFGNNNAAGVEIVAVERYL 670
Cdd:pfam19430 161 LVTATHMYCLREIASRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYL 225
TBC1D23_C-like cd20788
C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains ...
 574-688 1.45e-59

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: 195.92  E-value: 1.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 574 VNIQTWINKPDVKHHIPCNEVKETGHMFPSHLLITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKF 653
Cdd:cd20788    1 VNLSEWLKKPDVIASFECQEVKENGHMFPSYLLVTETHLYVLREIPDRKGYAKIVVRRPLSSIVKITSKKKHPELITFKY 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528482482 654 GNNNAAGVEIVAVERYLIPNAGDATKVIKQQIMKV 688
Cdd:cd20788   81 GTSDDDESEITDMDRFYIPKAGDATKAIKQAILKL 115
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 98-242 1.71e-16

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: 77.68  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   98 DLVSDVESVITFYCKSR-NVTFTPDLSwpHILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKGRP-----FHLFRLLL 171
Cdd:pfam00566  30 PGQNSLRRILKAYSIYNpDVGYCQGMN--FIAAPLLLVYLDEEDAFWCFVSLLENYLLRDFYTPDFPglkrdLYVFEELL 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528482482  172 QYHEPEFCSFLDTKKITPDSYAINWLGSLFsSHCLP-EVTQALWDVYLQQADPFLIFFLMLIILVNAKDNIL 242
Cdd:pfam00566 108 KKKLPKLYKHLKELGLDPDLFASQWFLTLF-AREFPlSTVLRIWDYFFLEGEKFVLFRVALAILKRFREELL 178
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 115-239 1.98e-10

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: 61.17  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   115 NVTFTPDLSWphILKPLLGLQLSRKDLYNCFYAIMNKYIPR----DCIVKGRPFHLFRLLLQYHEPEFCSFLDTKKITPD 190
Cdd:smart00164  88 EVGYCQGMNF--LAAPLLLVMEDEEDAFWCLVKLMERYGPNfylpDMSGLQLDLLQLDRLVKEYDPDLYKHLKDLGITPS 165

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528482482   191 SYAINWLGSLFSSHCLPEVTQALWDVYLQQADPFLIFFLMLIILVNAKD 239
Cdd:smart00164 166 LYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDV 214
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 324-435 2.35e-06

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 324 ANQLQPEGVRFFVVDCRPAEQYNAGHLSTAFHLD-SDLMLHNPSEFALSVKSLL--EAQKQSLESGSVAS----GEHLCF 396
Cdd:cd01446    8 AALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCcPTILRRRLQGGKILLQQLLscPEDRDRLRRGESLAvvvyDESSSD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528482482 397 MGSGReeEDMYMNMVLAHFLQKNKEF--VSIAKGGFMALQQ 435
Cdd:cd01446   88 RERLR--EDSTAESVLGKLLRKLQEGcsVYLLKGGFEQFSS 126
COG5210 COG5210
GTPase-activating protein [General function prediction only];
114-272 4.33e-04

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 43.25  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 114 RNVTFTPDLSWphILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKG-----RPFHLFRLLLQYHEPEFCSFLDTKKIT 188
Cdd:COG5210  297 PEVGYVQGMNF--LAAPLLLVLESEEQAFWCLVKLLKNYGLPGYFLKNlsglhRDLKVLDDLVEELDPELYEHLLREGVV 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 189 PDSYAINWLGSLFsSHCLP-EVTQALWDVYLQQADPFLIFFLMLIILVNAKDNILIQEGDNKEEIIKMLEQSPSLLEAED 267
Cdd:COG5210  375 LLMFAFRWFLTLF-VREFPlEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQLFLHSGKEAWSS 453


                 ....*
gi 528482482 268 IEDLF 272
Cdd:COG5210  454 ILKFR 458
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 336-380 1.07e-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: 38.62  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 528482482  336 VVDCRPAEQYNAGHLSTAFHLDSDLMLHNPSEFALSVKSLLEAQK 380
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLK 52
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 333-436 2.25e-03

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: 37.82  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   333 RFFVVDCRPAEQYNAGHLSTAFHLDSDLMLHNPSEFALSVKSLLEAQKQSLESGSVASgehLCFMGsgreeedMYMNMVL 412
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVV---YCRSG-------NRSAKAA 73

                           90       100
                   ....*....|....*....|....
gi 528482482   413 AHFLQKNKEFVSIAKGGFMALQQH 436
Cdd:smart00450  74 WLLRELGFKNVYLLDGGYKEWSAA 97
 
Name Accession Description Interval E-value
TBC1D23_C pfam19430
TBC1 domain family member 23 C-terminal; TBC1 domain family member 23 (TBC1D23) belongs to a ...
 447-670 6.17e-142

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: 413.79  E-value: 6.17e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  447 NVYVHWIVSTSGSHSSLSSADGE-LNSTDGKGVKSLVNKMTFALKSKSVNVKEKVISFIENTSTPVERMSFNLPWPDKGI 525
Cdd:pfam19430   1 NGYGHWIASTSGSRSSINSVDGEsLNGSGDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482  526 LERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSISDDDRKEIVNIQTWINKPDVKHHIPCNEVKETGHMFPSHL 605
Cdd:pfam19430  81 TERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482482  606 LITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKFGNNNAAGVEIVAVERYL 670
Cdd:pfam19430 161 LVTATHMYCLREIASRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYL 225
TBC1D23_C-like cd20788
C-terminal domain of TBC1 domain family member 23, and similar proteins; This family contains ...
 574-688 1.45e-59

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: 195.92  E-value: 1.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 574 VNIQTWINKPDVKHHIPCNEVKETGHMFPSHLLITATHMYCLREIAARKGFAYIQSRQALNSVVKITSKKKHPELITFKF 653
Cdd:cd20788    1 VNLSEWLKKPDVIASFECQEVKENGHMFPSYLLVTETHLYVLREIPDRKGYAKIVVRRPLSSIVKITSKKKHPELITFKY 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528482482 654 GNNNAAGVEIVAVERYLIPNAGDATKVIKQQIMKV 688
Cdd:cd20788   81 GTSDDDESEITDMDRFYIPKAGDATKAIKQAILKL 115
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 98-242 1.71e-16

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: 77.68  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   98 DLVSDVESVITFYCKSR-NVTFTPDLSwpHILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKGRP-----FHLFRLLL 171
Cdd:pfam00566  30 PGQNSLRRILKAYSIYNpDVGYCQGMN--FIAAPLLLVYLDEEDAFWCFVSLLENYLLRDFYTPDFPglkrdLYVFEELL 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528482482  172 QYHEPEFCSFLDTKKITPDSYAINWLGSLFsSHCLP-EVTQALWDVYLQQADPFLIFFLMLIILVNAKDNIL 242
Cdd:pfam00566 108 KKKLPKLYKHLKELGLDPDLFASQWFLTLF-AREFPlSTVLRIWDYFFLEGEKFVLFRVALAILKRFREELL 178
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 115-239 1.98e-10

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: 61.17  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   115 NVTFTPDLSWphILKPLLGLQLSRKDLYNCFYAIMNKYIPR----DCIVKGRPFHLFRLLLQYHEPEFCSFLDTKKITPD 190
Cdd:smart00164  88 EVGYCQGMNF--LAAPLLLVMEDEEDAFWCLVKLMERYGPNfylpDMSGLQLDLLQLDRLVKEYDPDLYKHLKDLGITPS 165

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528482482   191 SYAINWLGSLFSSHCLPEVTQALWDVYLQQADPFLIFFLMLIILVNAKD 239
Cdd:smart00164 166 LYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDV 214
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 324-435 2.35e-06

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 324 ANQLQPEGVRFFVVDCRPAEQYNAGHLSTAFHLD-SDLMLHNPSEFALSVKSLL--EAQKQSLESGSVAS----GEHLCF 396
Cdd:cd01446    8 AALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCcPTILRRRLQGGKILLQQLLscPEDRDRLRRGESLAvvvyDESSSD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528482482 397 MGSGReeEDMYMNMVLAHFLQKNKEF--VSIAKGGFMALQQ 435
Cdd:cd01446   88 RERLR--EDSTAESVLGKLLRKLQEGcsVYLLKGGFEQFSS 126
COG5210 COG5210
GTPase-activating protein [General function prediction only];
114-272 4.33e-04

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 43.25  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 114 RNVTFTPDLSWphILKPLLGLQLSRKDLYNCFYAIMNKYIPRDCIVKG-----RPFHLFRLLLQYHEPEFCSFLDTKKIT 188
Cdd:COG5210  297 PEVGYVQGMNF--LAAPLLLVLESEEQAFWCLVKLLKNYGLPGYFLKNlsglhRDLKVLDDLVEELDPELYEHLLREGVV 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482 189 PDSYAINWLGSLFsSHCLP-EVTQALWDVYLQQADPFLIFFLMLIILVNAKDNILIQEGDNKEEIIKMLEQSPSLLEAED 267
Cdd:COG5210  375 LLMFAFRWFLTLF-VREFPlEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLLKQLFLHSGKEAWSS 453


                 ....*
gi 528482482 268 IEDLF 272
Cdd:COG5210  454 ILKFR 458
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 336-380 1.07e-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: 38.62  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 528482482  336 VVDCRPAEQYNAGHLSTAFHLDSDLMLHNPSEFALSVKSLLEAQK 380
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLK 52
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 333-436 2.25e-03

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: 37.82  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482482   333 RFFVVDCRPAEQYNAGHLSTAFHLDSDLMLHNPSEFALSVKSLLEAQKQSLESGSVASgehLCFMGsgreeedMYMNMVL 412
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVV---YCRSG-------NRSAKAA 73

                           90       100
                   ....*....|....*....|....
gi 528482482   413 AHFLQKNKEFVSIAKGGFMALQQH 436
Cdd:smart00450  74 WLLRELGFKNVYLLDGGYKEWSAA 97
 
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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