NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19922922|ref|NP_611944|]
View 

uncharacterized protein Dmel_CG4707 [Drosophila melanogaster]

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
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-77 4.53e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 462262  Cd Length: 75  Bit Score: 47.84  E-value: 4.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922922     3 VCVLCLDSSNAGYGLQSEEGVRLNIRATIHKHFAFsEVLTAGGDAE-VCRECWNCVSSFEEFHQRVSCLHRQRSSD 77
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGI-ELDPNDLLPKqICERCLSKLQEFYSFRERCLESQELLQEL 75
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
455-574 5.86e-05

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 46.17  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922922 455 KYSCPE--CNKKIPTERKLKEHLRYMHDpeaAIICDKCGK---------TLRSQTNLKKHHELEHSE---KPRPKpdpvq 520
Cdd:COG5236 151 SFKCPKskCHRRCGSLKELKKHYKAQHG---FVLCSECIGnkkdfwneiRLFRSSTLRDHKNGGLEEegfKGHPL----- 222

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922922 521 CEICGTWLRHLSGLKQHMKTVHEppgdehRCHICNKTS-------TNSRALKRHIYHNHLC 574
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHE------ACHICDMVGpiryqyfKSYEDLEAHFRNAHYC 277
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 361-407 7.63e-03

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


The actual alignment was detected with superfamily member cd09392:

Pssm-ID: 413332 [Multi-domain]  Cd Length: 53  Bit Score: 35.03  E-value: 7.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19922922 361 YIECCGRKFHLrkalaehvlvhknpDHFMCSQCGRVFQDSRALEVHE 407
Cdd:cd09392  12 YITALGRKYHV--------------EHFTCSVCPTVFGPNDSYYEHE 44
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-77 4.53e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 47.84  E-value: 4.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922922     3 VCVLCLDSSNAGYGLQSEEGVRLNIRATIHKHFAFsEVLTAGGDAE-VCRECWNCVSSFEEFHQRVSCLHRQRSSD 77
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGI-ELDPNDLLPKqICERCLSKLQEFYSFRERCLESQELLQEL 75
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
455-574 5.86e-05

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 46.17  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922922 455 KYSCPE--CNKKIPTERKLKEHLRYMHDpeaAIICDKCGK---------TLRSQTNLKKHHELEHSE---KPRPKpdpvq 520
Cdd:COG5236 151 SFKCPKskCHRRCGSLKELKKHYKAQHG---FVLCSECIGnkkdfwneiRLFRSSTLRDHKNGGLEEegfKGHPL----- 222

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922922 521 CEICGTWLRHLSGLKQHMKTVHEppgdehRCHICNKTS-------TNSRALKRHIYHNHLC 574
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHE------ACHICDMVGpiryqyfKSYEDLEAHFRNAHYC 277
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-73 1.61e-03

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 37.49  E-value: 1.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922922      3 VCVLCLDSSNAGYGLQSEEGVRLnIRATIHKHFAFSEVLTAGGDAEVCRECWNCVSSFEEFHQRVSCLHRQ 73
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEAS-LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDEL 70
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
 361-407 7.63e-03

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 35.03  E-value: 7.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19922922 361 YIECCGRKFHLrkalaehvlvhknpDHFMCSQCGRVFQDSRALEVHE 407
Cdd:cd09392  12 YITALGRKYHV--------------EHFTCSVCPTVFGPNDSYYEHE 44
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-77 4.53e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 47.84  E-value: 4.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922922     3 VCVLCLDSSNAGYGLQSEEGVRLNIRATIHKHFAFsEVLTAGGDAE-VCRECWNCVSSFEEFHQRVSCLHRQRSSD 77
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGI-ELDPNDLLPKqICERCLSKLQEFYSFRERCLESQELLQEL 75
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
455-574 5.86e-05

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 46.17  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922922 455 KYSCPE--CNKKIPTERKLKEHLRYMHDpeaAIICDKCGK---------TLRSQTNLKKHHELEHSE---KPRPKpdpvq 520
Cdd:COG5236 151 SFKCPKskCHRRCGSLKELKKHYKAQHG---FVLCSECIGnkkdfwneiRLFRSSTLRDHKNGGLEEegfKGHPL----- 222

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922922 521 CEICGTWLRHLSGLKQHMKTVHEppgdehRCHICNKTS-------TNSRALKRHIYHNHLC 574
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHE------ACHICDMVGpiryqyfKSYEDLEAHFRNAHYC 277
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-73 1.61e-03

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 37.49  E-value: 1.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922922      3 VCVLCLDSSNAGYGLQSEEGVRLnIRATIHKHFAFSEVLTAGGDAEVCRECWNCVSSFEEFHQRVSCLHRQ 73
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEAS-LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDEL 70
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
 361-407 7.63e-03

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 35.03  E-value: 7.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19922922 361 YIECCGRKFHLrkalaehvlvhknpDHFMCSQCGRVFQDSRALEVHE 407
Cdd:cd09392  12 YITALGRKYHV--------------EHFTCSVCPTVFGPNDSYYEHE 44
 
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