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Conserved domains on  [gi|665391021|ref|NP_001285177|]
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radish, isoform J [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
870-1051 4.14e-74

Rap/ran-GAP;


:

Pssm-ID: 460463  Cd Length: 179  Bit Score: 244.34  E-value: 4.14e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   870 LDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGN 949
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   950 DIVCVVFLEADNTrFSPACIKSHFLHTFILVRVSARIKhKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKG--PMFREWLL 1027
Cdd:pfam02145   81 DIVNIVFNESGGP-FDPSTIKSQFNHVFIVVQPNLPDT-DNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA 158

                          170       180
                   ....*....|....*....|....
gi 665391021  1028 tkiVNGERASYSAPKFARMQERTR 1051
Cdd:pfam02145  159 ---INAERAALKSSSFAERLRRIR 179
BACK super family cl28903
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
 1506-1578 7.47e-11

BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal to a BTB domain, in a diverse set of architectures together with Kelch, MATH, and/or TAZ domains. It is involved in interactions with the Cullin3 (Cul3) ubiquitin ligase complex, as well as in homo-oligomerization. Most proteins containing the BACK domain are understood to function as adaptor proteins that play a role in ubiquitination of various substrates.


The actual alignment was detected with superfamily member cd18507:

Pssm-ID: 475122  Cd Length: 80  Bit Score: 59.83  E-value: 7.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1506 VCPMLISLENYYwRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCR-ELQTPEIRKFEAMLAWA 1578
Cdd:cd18507     5 VCALLASAERYD-QYKCTKTLVQKVLEFVDKHGTDVLNLPEFLLLPEHVVRLILSRdSLGADEMTKFQAALAWS 77
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 1442-1501 7.88e-08

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


:

Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 51.92  E-value: 7.88e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFL 1501
Cdd:smart00225   38 KSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLKLL 97
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 1266-1321 7.84e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.


The actual alignment was detected with superfamily member cd18294:

Pssm-ID: 453885 [Multi-domain]  Cd Length: 111  Bit Score: 43.77  E-value: 7.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391021 1266 SCLTNAHLFDVVFLVGQSKQKarFIGVRAILGVRSRVFQEMLYgIQTGFGSPQIPV 1321
Cdd:cd18294     7 SLINNPEFSDVKFLVGPERQE--IFAHKCILAARCEVFRAMFL-TGPQKESTQSPL 59
PHA03309 super family cl29689
transcriptional regulator ICP4; Provisional
 184-516 9.56e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03309:

Pssm-ID: 165564 [Multi-domain]  Cd Length: 2033  Bit Score: 44.46  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  184 RHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESylSSSRRDSNVAGR------VTTPPPPGKYQMTKKRDSLAAPE 257
Cdd:PHA03309 1546 RHADRRRSTKGPQRPGGKRPRSSSSSSSASHDRSPSS--SSRRRDGRPSSRrrpsrrMSARPPSRPPAAVILRASWRYAE 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  258 fpNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSAC-QALPPPTIITSSVTP-PATSPTAPK--GRRD-SQT 332
Cdd:PHA03309 1624 --EVAREMLDAAASRFDEADGEDPLPPAACGGKPIAPETLVALCeQRGRGPTSLPRAPTPrSGEALAAPRrsGAKDpRQG 1701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  333 Q-CGRVNRRDSKAGVSPeRAPRLQRLQRQATAFDEGCLPggSRRGSqPALSPDPPD-DCERRT--SRRDSlsPDSASRGG 408
Cdd:PHA03309 1702 QyCPSARRSEAPHSPSP-RDVALRLLERQQELNRQLLLE--LRRGS-CEISPSPRRrDAEGRRfgCRQDD--DDGYDYEG 1775

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  409 RRDSRTHLSPDRSHERDGSPRRhtlRRQSSSA-------ARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQ 481
Cdd:PHA03309 1776 GRESPERVLGRRQSRRDSVPVR---RRSGAANcggrwmiSAGRSSSSSSSSSSSSSSSPSSRPSRSATPSLSPSPSPPRR 1852

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 665391021  482 STTEEILIARgfRRQSTTEEMIRCRNFRRQSSQSD 516
Cdd:PHA03309 1853 APVDRSRSGR--RRERDRPSANPFRWAPRQRSRAD 1885
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 560-600 1.72e-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).


:

Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 38.07  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 665391021  560 YDNNHYHEECLRCNSCGLNLTGpnqKRARRFKNQILCDLHF 600
Cdd:cd08368    16 ALGKKWHPECFKCAECGKPLGG---DSFYEKDGKPYCEKCY 53
 
Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
870-1051 4.14e-74

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 244.34  E-value: 4.14e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   870 LDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGN 949
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   950 DIVCVVFLEADNTrFSPACIKSHFLHTFILVRVSARIKhKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKG--PMFREWLL 1027
Cdd:pfam02145   81 DIVNIVFNESGGP-FDPSTIKSQFNHVFIVVQPNLPDT-DNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA 158

                          170       180
                   ....*....|....*....|....
gi 665391021  1028 tkiVNGERASYSAPKFARMQERTR 1051
Cdd:pfam02145  159 ---INAERAALKSSSFAERLRRIR 179
BACK_GPRS_like cd18507
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster serine-enriched ...
 1506-1578 7.47e-11

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins; The family includes uncharacterized Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins.


Pssm-ID: 350582  Cd Length: 80  Bit Score: 59.83  E-value: 7.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1506 VCPMLISLENYYwRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCR-ELQTPEIRKFEAMLAWA 1578
Cdd:cd18507     5 VCALLASAERYD-QYKCTKTLVQKVLEFVDKHGTDVLNLPEFLLLPEHVVRLILSRdSLGADEMTKFQAALAWS 77
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 1442-1501 7.88e-08

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 51.92  E-value: 7.88e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFL 1501
Cdd:smart00225   38 KSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLKLL 97
BTB_POZ_KLHL27_IPP cd18256
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1442-1505 3.58e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349565 [Multi-domain]  Cd Length: 125  Bit Score: 47.78  E-value: 3.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACfhhCkQFLRIEV 1505
Cdd:cd18256    59 KDVVQIHGVEPDIFHILLDFIYTGVVEVTVSNVQELLVAADMLQLTEVVEIC---C-EFLKGQL 118
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 1442-1501 5.00e-06

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 46.87  E-value: 5.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCvSIPGLLCAAEHYDLPELLQACFHHCKQFL 1501
Cdd:pfam00651   49 VSEITLDDVSPEDFEALLEFMYTGKLISEE-NVDDLLAAADKLQIPSLVDKCEEFLIKSL 107
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1266-1321 7.84e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 43.77  E-value: 7.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391021 1266 SCLTNAHLFDVVFLVGQSKQKarFIGVRAILGVRSRVFQEMLYgIQTGFGSPQIPV 1321
Cdd:cd18294     7 SLINNPEFSDVKFLVGPERQE--IFAHKCILAARCEVFRAMFL-TGPQKESTQSPL 59
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 1519-1621 4.76e-04

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 41.17  E-value: 4.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   1519 RYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCR-ELQTP-EIRKFEAMLAWAQHKVGKLKNHpnkdtqfe 1596
Cdd:smart00875    9 DAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSdDLNVSsEEEVFEAVLRWVKHDPEKRREH-------- 80

                            90       100
                    ....*....|....*....|....*
gi 665391021   1597 feciMERLTRDLNLCRISPSELLTV 1621
Cdd:smart00875   81 ----LPELLEHVRLPLLSPDYLLEV 101
PHA03309 PHA03309
transcriptional regulator ICP4; Provisional
 184-516 9.56e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 165564 [Multi-domain]  Cd Length: 2033  Bit Score: 44.46  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  184 RHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESylSSSRRDSNVAGR------VTTPPPPGKYQMTKKRDSLAAPE 257
Cdd:PHA03309 1546 RHADRRRSTKGPQRPGGKRPRSSSSSSSASHDRSPSS--SSRRRDGRPSSRrrpsrrMSARPPSRPPAAVILRASWRYAE 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  258 fpNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSAC-QALPPPTIITSSVTP-PATSPTAPK--GRRD-SQT 332
Cdd:PHA03309 1624 --EVAREMLDAAASRFDEADGEDPLPPAACGGKPIAPETLVALCeQRGRGPTSLPRAPTPrSGEALAAPRrsGAKDpRQG 1701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  333 Q-CGRVNRRDSKAGVSPeRAPRLQRLQRQATAFDEGCLPggSRRGSqPALSPDPPD-DCERRT--SRRDSlsPDSASRGG 408
Cdd:PHA03309 1702 QyCPSARRSEAPHSPSP-RDVALRLLERQQELNRQLLLE--LRRGS-CEISPSPRRrDAEGRRfgCRQDD--DDGYDYEG 1775

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  409 RRDSRTHLSPDRSHERDGSPRRhtlRRQSSSA-------ARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQ 481
Cdd:PHA03309 1776 GRESPERVLGRRQSRRDSVPVR---RRSGAANcggrwmiSAGRSSSSSSSSSSSSSSSPSSRPSRSATPSLSPSPSPPRR 1852

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 665391021  482 STTEEILIARgfRRQSTTEEMIRCRNFRRQSSQSD 516
Cdd:PHA03309 1853 APVDRSRSGR--RRERDRPSANPFRWAPRQRSRAD 1885
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 560-600 1.72e-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).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 38.07  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 665391021  560 YDNNHYHEECLRCNSCGLNLTGpnqKRARRFKNQILCDLHF 600
Cdd:cd08368    16 ALGKKWHPECFKCAECGKPLGG---DSFYEKDGKPYCEKCY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 554-599 1.83e-03

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 38.13  E-value: 1.83e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665391021    554 TEPSPLYDNNHYHEECLRCNSCGLNLTGpnqKRARRFKNQILCDLH 599
Cdd:smart00132   12 TERVLRALGKVWHPECFKCATCGKPLSG---DTFFEKDGKLYCKDC 54
 
Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
870-1051 4.14e-74

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 244.34  E-value: 4.14e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   870 LDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGN 949
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   950 DIVCVVFLEADNTrFSPACIKSHFLHTFILVRVSARIKhKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKG--PMFREWLL 1027
Cdd:pfam02145   81 DIVNIVFNESGGP-FDPSTIKSQFNHVFIVVQPNLPDT-DNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA 158

                          170       180
                   ....*....|....*....|....
gi 665391021  1028 tkiVNGERASYSAPKFARMQERTR 1051
Cdd:pfam02145  159 ---INAERAALKSSSFAERLRRIR 179
BACK_GPRS_like cd18507
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster serine-enriched ...
 1506-1578 7.47e-11

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins; The family includes uncharacterized Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins.


Pssm-ID: 350582  Cd Length: 80  Bit Score: 59.83  E-value: 7.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1506 VCPMLISLENYYwRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCR-ELQTPEIRKFEAMLAWA 1578
Cdd:cd18507     5 VCALLASAERYD-QYKCTKTLVQKVLEFVDKHGTDVLNLPEFLLLPEHVVRLILSRdSLGADEMTKFQAALAWS 77
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 1442-1501 7.88e-08

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 51.92  E-value: 7.88e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFL 1501
Cdd:smart00225   38 KSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLKLL 97
BTB_POZ_KLHL27_IPP cd18256
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1442-1505 3.58e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349565 [Multi-domain]  Cd Length: 125  Bit Score: 47.78  E-value: 3.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACfhhCkQFLRIEV 1505
Cdd:cd18256    59 KDVVQIHGVEPDIFHILLDFIYTGVVEVTVSNVQELLVAADMLQLTEVVEIC---C-EFLKGQL 118
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 1442-1501 5.00e-06

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 46.87  E-value: 5.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCvSIPGLLCAAEHYDLPELLQACFHHCKQFL 1501
Cdd:pfam00651   49 VSEITLDDVSPEDFEALLEFMYTGKLISEE-NVDDLLAAADKLQIPSLVDKCEEFLIKSL 107
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1441-1493 5.93e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 46.86  E-value: 5.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665391021 1441 AQTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQAC 1493
Cdd:cd18294    55 TQSPLVLSDIEPEVFRAVLEFIYTNCVTLSNHTVIEVLAAAVEYGLDELRKLC 107
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1442-1484 4.55e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349497 [Multi-domain]  Cd Length: 82  Bit Score: 43.31  E-value: 4.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665391021 1442 QTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHY 1484
Cdd:cd18186    40 SSEIELDDVSPEAFEALLDYIYTGELELSEENVEELLAAADKL 82
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1266-1321 7.84e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 43.77  E-value: 7.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391021 1266 SCLTNAHLFDVVFLVGQSKQKarFIGVRAILGVRSRVFQEMLYgIQTGFGSPQIPV 1321
Cdd:cd18294     7 SLINNPEFSDVKFLVGPERQE--IFAHKCILAARCEVFRAMFL-TGPQKESTQSPL 59
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 1519-1621 4.76e-04

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 41.17  E-value: 4.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021   1519 RYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCR-ELQTP-EIRKFEAMLAWAQHKVGKLKNHpnkdtqfe 1596
Cdd:smart00875    9 DAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSdDLNVSsEEEVFEAVLRWVKHDPEKRREH-------- 80

                            90       100
                    ....*....|....*....|....*
gi 665391021   1597 feciMERLTRDLNLCRISPSELLTV 1621
Cdd:smart00875   81 ----LPELLEHVRLPLLSPDYLLEV 101
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 1453-1505 8.25e-04

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349609 [Multi-domain]  Cd Length: 108  Bit Score: 40.69  E-value: 8.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665391021 1453 DTFRVLLDYLHTGTCP-LTCVSIPGLLCAAEHYDLPELLqacfHHCKQFLRIEV 1505
Cdd:cd18300    59 ETFLALLEYLYTDQAPiLEDGDCVGLIVLANRLCLPRLV----ALCEQYIVKEL 108
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1250-1309 8.79e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349596 [Multi-domain]  Cd Length: 119  Bit Score: 40.68  E-value: 8.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021 1250 DQLAKDFTRVFLNEEPScltnahlfDVVFLVgqskQKARFIGVRAILGVRSRVFQEMLYG 1309
Cdd:cd18287     7 HFLSEDIGALFLNEEYS--------DVTFVV----EEKRFPAHRVILAARSEYFRALLYG 54
PHA03309 PHA03309
transcriptional regulator ICP4; Provisional
 184-516 9.56e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 165564 [Multi-domain]  Cd Length: 2033  Bit Score: 44.46  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  184 RHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESylSSSRRDSNVAGR------VTTPPPPGKYQMTKKRDSLAAPE 257
Cdd:PHA03309 1546 RHADRRRSTKGPQRPGGKRPRSSSSSSSASHDRSPSS--SSRRRDGRPSSRrrpsrrMSARPPSRPPAAVILRASWRYAE 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  258 fpNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSAC-QALPPPTIITSSVTP-PATSPTAPK--GRRD-SQT 332
Cdd:PHA03309 1624 --EVAREMLDAAASRFDEADGEDPLPPAACGGKPIAPETLVALCeQRGRGPTSLPRAPTPrSGEALAAPRrsGAKDpRQG 1701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  333 Q-CGRVNRRDSKAGVSPeRAPRLQRLQRQATAFDEGCLPggSRRGSqPALSPDPPD-DCERRT--SRRDSlsPDSASRGG 408
Cdd:PHA03309 1702 QyCPSARRSEAPHSPSP-RDVALRLLERQQELNRQLLLE--LRRGS-CEISPSPRRrDAEGRRfgCRQDD--DDGYDYEG 1775

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  409 RRDSRTHLSPDRSHERDGSPRRhtlRRQSSSA-------ARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQ 481
Cdd:PHA03309 1776 GRESPERVLGRRQSRRDSVPVR---RRSGAANcggrwmiSAGRSSSSSSSSSSSSSSSPSSRPSRSATPSLSPSPSPPRR 1852

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 665391021  482 STTEEILIARgfRRQSTTEEMIRCRNFRRQSSQSD 516
Cdd:PHA03309 1853 APVDRSRSGR--RRERDRPSANPFRWAPRQRSRAD 1885
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 188-483 1.37e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  188 RRESGAVEEQPSVSVPVVVECSKSASRRGSGESYLSSSRRDSnvagrVTTPPPPGKYQMTKKRDSLAAPefpnfRQEQRP 267
Cdd:PHA03307  141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEET-----ARAPSSPPAEPPPSTPPAAASP-----RPPRRS 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  268 STSSAGSCSDHSMPLIST----HSSTHHLAHQQ-------VDSACqALPPPTIITSSVTPPATSPTAPKGRRdsqtqCGR 336
Cdd:PHA03307  211 SPISASASSPAPAPGRSAaddaGASSSDSSSSEssgcgwgPENEC-PLPRPAPITLPTRIWEASGWNGPSSR-----PGP 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  337 VNRRDSKAGVSPERAPRlqrlqrqatafDEGCLPGGSRRGSQPALSPDPPDDCERrTSRRDSLSPDSASRGGRRDSRTHL 416
Cdd:PHA03307  285 ASSSSSPRERSPSPSPS-----------SPGSGPAPSSPRASSSSSSSRESSSSS-TSSSSESSRGAAVSPGPSPSRSPS 352

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665391021  417 SPDRSHERDGSPRRhtlRRQSssaarsprspdSNSCCSSRDPSPcSRPQTQTTVEQNQRPAIRRQST 483
Cdd:PHA03307  353 PSRPPPPADPSSPR---KRPR-----------PSRAPSSPAASA-GRPTRRRARAAVAGRARRRDAT 404
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 560-600 1.72e-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).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 38.07  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 665391021  560 YDNNHYHEECLRCNSCGLNLTGpnqKRARRFKNQILCDLHF 600
Cdd:cd08368    16 ALGKKWHPECFKCAECGKPLGG---DSFYEKDGKPYCEKCY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 554-599 1.83e-03

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 38.13  E-value: 1.83e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665391021    554 TEPSPLYDNNHYHEECLRCNSCGLNLTGpnqKRARRFKNQILCDLH 599
Cdd:smart00132   12 TERVLRALGKVWHPECFKCATCGKPLSG---DTFFEKDGKLYCKDC 54
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 1448-1484 2.43e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 38.69  E-value: 2.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 665391021 1448 IEFDPDTFRVLLDYLHTGT--CPLTCVSIPGLLCAAEHY 1484
Cdd:cd18316    45 IDRDPELFRHILNFLRTGKlpLPSDFVELEELLAEAEFY 83
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 1452-1493 2.49e-03

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. In vertebrates, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349608 [Multi-domain]  Cd Length: 103  Bit Score: 39.12  E-value: 2.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665391021 1452 PDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQAC 1493
Cdd:cd18299    57 PEAFRRVLEFLYTGVLDENEDDLKELKDAAELLELFDLVMMC 98
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 228-408 3.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  228 DSNVAGRVTTPPPPGKYQMTKKRDSLAAPEFPNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSACQALPPP 307
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  308 TIITSSVTPPATSPTAPKGRRDSQTqcGRVNRRDSKAGVSPERAPRLQRLQRQATAFDEGCLPGGSRRGSQPALSPDPPD 387
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPA--GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         170       180
                  ....*....|....*....|.
gi 665391021  388 DCERRTSRRDSLSPDSASRGG 408
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAA 768
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 238-498 4.58e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  238 PPPPGKYQMTKKRDSLAAPEFP-------NFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSACQALPPPTII 310
Cdd:PHA03307  129 SPAPDLSEMLRPVGSPGPPPAAsppaagaSPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  311 TSSVTPPATSPTAPKGRRDSQTQCGRVN-------RRDSKAGVSPERAPRLQRLQRQATAFDEGCLPGGSRRGSQPALSP 383
Cdd:PHA03307  209 RSSPISASASSPAPAPGRSAADDAGASSsdsssseSSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021  384 DPPDDCERRTSRRDSLSPDSASRggrRDSRTHLSPDRSHERDGSPRRHTLRRQS-----SSAARSPRSPD--SNSCCSSR 456
Cdd:PHA03307  289 SSPRERSPSPSPSSPGSGPAPSS---PRASSSSSSSRESSSSSTSSSSESSRGAavspgPSPSRSPSPSRppPPADPSSP 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 665391021  457 DPSPCSRPQTQTTVEQNQRPAIRRQSTTeeiLIARGFRRQST 498
Cdd:PHA03307  366 RKRPRPSRAPSSPAASAGRPTRRRARAA---VAGRARRRDAT 404
BACK_BTBD9 cd14822
BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 9 (BTBD9); ...
 1501-1605 5.65e-03

BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation.


Pssm-ID: 350518 [Multi-domain]  Cd Length: 101  Bit Score: 37.98  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391021 1501 LRIEVVCpMLISLENYYwrytSASELVNMILSFVESKAHSLFKCPEFLHLSE-SMVQMIMCRELQTPEIRKFEAMLAWAQ 1579
Cdd:cd14822     1 LNIRNVC-LIYDVASLY----SLDDLCQTCCQFMDRNAQEVLSSEGFLTLSKsALKELLSRDSFCAPEVDIFNAVRRWCE 75

                          90       100
                  ....*....|....*....|....*...
gi 665391021 1580 HkvgklknhpNKDTQFEFECIME--RLT 1605
Cdd:cd14822    76 H---------NPDSKEDAKEILEavRLP 94
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
 1449-1493 9.48e-03

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins; Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349623 [Multi-domain]  Cd Length: 96  Bit Score: 37.32  E-value: 9.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 665391021 1449 EFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQAC 1493
Cdd:cd18314    52 DVEPEIFETVLKYMYTGQVTLSEENVLDLLMLASKYQVPDLEKLC 96
 
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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