NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462506747|ref|XP_054191403|]
View 

calmodulin-binding transcription activator 1 isoform X10 [Homo sapiens]

Protein Classification

CG-1 and TIG domain-containing protein( domain architecture ID 13931160)

CG-1 and TIG domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
37-153 1.71e-73

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


:

Pssm-ID: 198144  Cd Length: 118  Bit Score: 240.00  E-value: 1.71e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747    37 LPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKY-RKDGYCWKKRKDGKTTREDHMKLKVQGV 115
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2462506747   116 ECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVP 153
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
843-922 1.11e-09

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


:

Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747  843 VTDYSPEWSYPEGGVKVLITGP-WQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNN-QIISNSVVF 920
Cdd:pfam01833    3 ITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGgGISSSPLTF 82

                   ..
gi 2462506747  921 EY 922
Cdd:pfam01833   83 TY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1028-1133 2.10e-09

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1028 IHSKTFRGMTLLHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLykWDRRA- 1106
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLL------------LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL--LEAGAd 178
                           90       100
                   ....*....|....*....|....*..
gi 2462506747 1107 ISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLL 205
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1556-1590 3.21e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.75  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462506747 1556 EQKKFQQSRRAAVLIQKYYRSYKkcgKRRQARRTA 1590
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYK---VRKELKKKK 32
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1489-1639 9.56e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 9.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1489 HEQRELYEAARLvqtafRKYKGRpLREQQEVAAAVIQRC---YRKYKQYALYKKMTQAAILIQSKFRSYYEQKKFQQSRR 1565
Cdd:pfam13868   79 EEQIEEREQKRQ-----EEYEEK-LQEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEERE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1566 AAVLIQKY-------YRSYKKcgKRRQARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLR-----RCRHRVKEL----KK 1629
Cdd:pfam13868  153 EDERILEYlkekaerEEEREA--EREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEReeaeKK 230
                          170
                   ....*....|
gi 2462506747 1630 AKELEDIQQH 1639
Cdd:pfam13868  231 ARQRQELQQA 240
 
Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
37-153 1.71e-73

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 198144  Cd Length: 118  Bit Score: 240.00  E-value: 1.71e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747    37 LPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKY-RKDGYCWKKRKDGKTTREDHMKLKVQGV 115
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2462506747   116 ECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVP 153
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
41-152 3.10e-57

CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues containing a predicted bipartite NLS and named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 461077  Cd Length: 114  Bit Score: 193.25  E-value: 3.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747   41 RHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKY-RKDGYCWKKRKDGKTTREDHMKLKVQGVECLY 119
Cdd:pfam03859    1 KTRWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIH 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462506747  120 GCYVHSSIIPTFHRRCYWLLQNP-DIVLVHYLNV 152
Cdd:pfam03859   81 CYYAHSEDNPTFQRRIYWLLDSDyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
843-922 1.11e-09

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747  843 VTDYSPEWSYPEGGVKVLITGP-WQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNN-QIISNSVVF 920
Cdd:pfam01833    3 ITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGgGISSSPLTF 82

                   ..
gi 2462506747  921 EY 922
Cdd:pfam01833   83 TY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1028-1133 2.10e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1028 IHSKTFRGMTLLHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLykWDRRA- 1106
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLL------------LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL--LEAGAd 178
                           90       100
                   ....*....|....*....|....*..
gi 2462506747 1107 ISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1039-1131 1.10e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1039 LHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAA-VVLYKWDRRAisipDSLGRLP 1117
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNL----KDNGRTA 64
                           90
                   ....*....|....
gi 2462506747 1118 LGIARSRGHVKLAE 1131
Cdd:pfam12796   65 LHYAARSGHLEIVK 78
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1556-1590 3.21e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.75  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462506747 1556 EQKKFQQSRRAAVLIQKYYRSYKkcgKRRQARRTA 1590
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYK---VRKELKKKK 32
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1489-1639 9.56e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 9.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1489 HEQRELYEAARLvqtafRKYKGRpLREQQEVAAAVIQRC---YRKYKQYALYKKMTQAAILIQSKFRSYYEQKKFQQSRR 1565
Cdd:pfam13868   79 EEQIEEREQKRQ-----EEYEEK-LQEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEERE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1566 AAVLIQKY-------YRSYKKcgKRRQARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLR-----RCRHRVKEL----KK 1629
Cdd:pfam13868  153 EDERILEYlkekaerEEEREA--EREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEReeaeKK 230
                          170
                   ....*....|
gi 2462506747 1630 AKELEDIQQH 1639
Cdd:pfam13868  231 ARQRQELQQA 240
 
Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
37-153 1.71e-73

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 198144  Cd Length: 118  Bit Score: 240.00  E-value: 1.71e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747    37 LPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKY-RKDGYCWKKRKDGKTTREDHMKLKVQGV 115
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2462506747   116 ECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVP 153
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
41-152 3.10e-57

CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues containing a predicted bipartite NLS and named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 461077  Cd Length: 114  Bit Score: 193.25  E-value: 3.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747   41 RHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKY-RKDGYCWKKRKDGKTTREDHMKLKVQGVECLY 119
Cdd:pfam03859    1 KTRWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIH 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462506747  120 GCYVHSSIIPTFHRRCYWLLQNP-DIVLVHYLNV 152
Cdd:pfam03859   81 CYYAHSEDNPTFQRRIYWLLDSDyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
843-922 1.11e-09

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747  843 VTDYSPEWSYPEGGVKVLITGP-WQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNN-QIISNSVVF 920
Cdd:pfam01833    3 ITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGgGISSSPLTF 82

                   ..
gi 2462506747  921 EY 922
Cdd:pfam01833   83 TY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1028-1133 2.10e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1028 IHSKTFRGMTLLHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLykWDRRA- 1106
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLL------------LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL--LEAGAd 178
                           90       100
                   ....*....|....*....|....*..
gi 2462506747 1107 ISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1022-1133 2.50e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1022 AKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYk 1101
Cdd:COG0666     74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLL------------LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL- 140
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462506747 1102 wDRRA-ISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:COG0666    141 -EAGAdVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1039-1131 1.10e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1039 LHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAA-VVLYKWDRRAisipDSLGRLP 1117
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNL----KDNGRTA 64
                           90
                   ....*....|....
gi 2462506747 1118 LGIARSRGHVKLAE 1131
Cdd:pfam12796   65 LHYAARSGHLEIVK 78
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1028-1101 1.80e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.80e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506747 1028 IHSKTFRGMTLLHLAAAQGYATLIQTLIKwrtkHADsidlelevdpLNVDHFSCTPLMWACALGHLEAAVVLYK 1101
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE----HAD----------VNLKDNGRTALHYAARSGHLEIVKLLLE 82
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1028-1144 2.27e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.03  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1028 IHSKTFRGMTLLHLAAAQGYATLIQTLikwrtkhadsidLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYKwDRRAI 1107
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLL------------LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADL 245
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462506747 1108 SIPDSLGRLPLGIARSRGHVKLAECLEHLQRDEQAQL 1144
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1556-1590 3.21e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.75  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462506747 1556 EQKKFQQSRRAAVLIQKYYRSYKkcgKRRQARRTA 1590
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYK---VRKELKKKK 32
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1022-1133 4.61e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.09  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1022 AKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLIKWRTKHADSIDLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYk 1101
Cdd:COG0666     29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL- 107
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462506747 1102 wDRRA-ISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:COG0666    108 -EAGAdVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
1082-1133 4.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 4.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462506747 1082 TPLMWACALGHLEAAVVLY--KWDrraISIPDSLGRLPLGIARSRGHVKLAECL 1133
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLekGAD---INAVDGNGETALHFAASNGNVEVLKLL 53
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1489-1639 9.56e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 9.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1489 HEQRELYEAARLvqtafRKYKGRpLREQQEVAAAVIQRC---YRKYKQYALYKKMTQAAILIQSKFRSYYEQKKFQQSRR 1565
Cdd:pfam13868   79 EEQIEEREQKRQ-----EEYEEK-LQEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEERE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506747 1566 AAVLIQKY-------YRSYKKcgKRRQARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLR-----RCRHRVKEL----KK 1629
Cdd:pfam13868  153 EDERILEYlkekaerEEEREA--EREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEReeaeKK 230
                          170
                   ....*....|
gi 2462506747 1630 AKELEDIQQH 1639
Cdd:pfam13868  231 ARQRQELQQA 240
 
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