NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462540582|ref|XP_054232200|]
View 

zinc finger FYVE domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 174-410 3.71e-59

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


:

Pssm-ID: 206650  Cd Length: 224  Bit Score: 194.08  E-value: 3.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 174 CKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGrEVFKTSPTQESCTVGVWAAYDPV-------HKVAVIDTEGLLGATVNL 246
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTS-DGFDVMDTSQQTTKGIWMWSDPFkdtdgkkHAVLLLDTEGTDGRERGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 247 -SQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAylkhftkelkattarcgldvpLSTLGPAVIIFHETVHTQ 325
Cdd:cd01851    80 fENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTA---------------------LETLGLAGLHNFSKPKPL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 326 LLGSDHPSEVPEKLIQD-----RFRKLGRFPEAFSSIHYKGTrtynPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKAL 400
Cdd:cd01851   139 LLFVVRDFTGPTPLEGLdvtekSETLIEELNKIWSSIRKPFT----PITCFVLPHPGLLHKLLQNDGRLKDLPPEFRKAL 214

                         250
                  ....*....|
gi 2462540582 401 KALSDRFSGE 410
Cdd:cd01851   215 KALRQRFFSS 224
Bbox1_ZFYVE1_rpt2 cd19820
second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 69-122 1.29e-28

second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


:

Pssm-ID: 380878  Cd Length: 59  Bit Score: 107.35  E-value: 1.29e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540582  69 PYCDLCKGLSGHL-----PGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYN 122
Cdd:cd19820     1 PYCDSCKGGNGNSmhsstAGSRQRAAVRCQSCKINLCPECQKRTHSGGNKRKHPVTVYP 59
Bbox1_ZFYVE1_rpt1 cd19819
first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 16-63 5.08e-24

first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


:

Pssm-ID: 380877  Cd Length: 48  Bit Score: 94.50  E-value: 5.08e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462540582  16 LMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRL 63
Cdd:cd19819     1 LMCQESYACSGSDEAVFECDECGSLQCQRCEKELHQQERLRNHERTRI 48
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 174-410 3.71e-59

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 194.08  E-value: 3.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 174 CKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGrEVFKTSPTQESCTVGVWAAYDPV-------HKVAVIDTEGLLGATVNL 246
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTS-DGFDVMDTSQQTTKGIWMWSDPFkdtdgkkHAVLLLDTEGTDGRERGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 247 -SQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAylkhftkelkattarcgldvpLSTLGPAVIIFHETVHTQ 325
Cdd:cd01851    80 fENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTA---------------------LETLGLAGLHNFSKPKPL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 326 LLGSDHPSEVPEKLIQD-----RFRKLGRFPEAFSSIHYKGTrtynPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKAL 400
Cdd:cd01851   139 LLFVVRDFTGPTPLEGLdvtekSETLIEELNKIWSSIRKPFT----PITCFVLPHPGLLHKLLQNDGRLKDLPPEFRKAL 214

                         250
                  ....*....|
gi 2462540582 401 KALSDRFSGE 410
Cdd:cd01851   215 KALRQRFFSS 224
Bbox1_ZFYVE1_rpt2 cd19820
second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 69-122 1.29e-28

second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380878  Cd Length: 59  Bit Score: 107.35  E-value: 1.29e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540582  69 PYCDLCKGLSGHL-----PGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYN 122
Cdd:cd19820     1 PYCDSCKGGNGNSmhsstAGSRQRAAVRCQSCKINLCPECQKRTHSGGNKRKHPVTVYP 59
Bbox1_ZFYVE1_rpt1 cd19819
first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 16-63 5.08e-24

first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380877  Cd Length: 48  Bit Score: 94.50  E-value: 5.08e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462540582  16 LMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRL 63
Cdd:cd19819     1 LMCQESYACSGSDEAVFECDECGSLQCQRCEKELHQQERLRNHERTRI 48
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 174-410 3.71e-59

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 194.08  E-value: 3.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 174 CKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGrEVFKTSPTQESCTVGVWAAYDPV-------HKVAVIDTEGLLGATVNL 246
Cdd:cd01851     1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTS-DGFDVMDTSQQTTKGIWMWSDPFkdtdgkkHAVLLLDTEGTDGRERGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 247 -SQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAylkhftkelkattarcgldvpLSTLGPAVIIFHETVHTQ 325
Cdd:cd01851    80 fENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTA---------------------LETLGLAGLHNFSKPKPL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 326 LLGSDHPSEVPEKLIQD-----RFRKLGRFPEAFSSIHYKGTrtynPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKAL 400
Cdd:cd01851   139 LLFVVRDFTGPTPLEGLdvtekSETLIEELNKIWSSIRKPFT----PITCFVLPHPGLLHKLLQNDGRLKDLPPEFRKAL 214

                         250
                  ....*....|
gi 2462540582 401 KALSDRFSGE 410
Cdd:cd01851   215 KALRQRFFSS 224
Bbox1_ZFYVE1_rpt2 cd19820
second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 69-122 1.29e-28

second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380878  Cd Length: 59  Bit Score: 107.35  E-value: 1.29e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540582  69 PYCDLCKGLSGHL-----PGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYN 122
Cdd:cd19820     1 PYCDSCKGGNGNSmhsstAGSRQRAAVRCQSCKINLCPECQKRTHSGGNKRKHPVTVYP 59
Bbox1_ZFYVE1_rpt1 cd19819
first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) ...
 16-63 5.08e-24

first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins; ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380877  Cd Length: 48  Bit Score: 94.50  E-value: 5.08e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462540582  16 LMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRL 63
Cdd:cd19819     1 LMCQESYACSGSDEAVFECDECGSLQCQRCEKELHQQERLRNHERTRI 48
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 71-116 1.80e-03

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 36.32  E-value: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462540582  71 CDLCKglsghlpgvRQRAIVRCQTCKINLCLECQKRTHSGGNKRRH 116
Cdd:cd19757     2 CDECE---------EREATVYCLECEEFLCDDCSDAIHRRGKLTRS 38
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 187-272 3.30e-03

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 39.22  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 187 GNTGDGKSHTLNHTFfyGREVFKTSPTQESCT-----VGVWAAYdpvhKVAVIDTEGLLGAT---VN---LSQRTRLLLK 255
Cdd:cd01853    38 GKTGVGKSSTINSIF--GERKVSVSAFQSETLrprevSRTVDGF----KLNIIDTPGLLESQdqrVNrkiLSIIKRFLKK 111

                          90
                  ....*....|....*..
gi 2462540582 256 VLAisDLVIYrthADRL 272
Cdd:cd01853   112 KTI--DVVLY---VDRL 123
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 185-265 4.80e-03

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 37.82  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540582 185 IFGNTGDGKSHTLNHtfFYGREVFKTSPTQES---CTVGVWAAYDPVHKVAVIDTEGLLGAtvNLSQRTRLLLKVLAISD 261
Cdd:cd00882     2 VVGRGGVGKSSLLNA--LLGGEVGEVSDVPGTtrdPDVYVKELDKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGAD 77


                  ....
gi 2462540582 262 LVIY 265
Cdd:cd00882    78 LILL 81
Bbox2_MYCBP2 cd19799
B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, ...
 26-65 7.26e-03

B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380857  Cd Length: 50  Bit Score: 34.68  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462540582  26 GTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKP 65
Cdd:cd19799     9 GETAAIIFCCDCGNYLCAECDRFLHLHRKNRSHQRQVFKE 48
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH