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Conserved domains on  [gi|30697970|ref|NP_201227|]
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Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domain [Arabidopsis thaliana]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13692038)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 23-135 3.61e-71

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: 231.39  E-value: 3.61e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970     23 QHRWLRPAEICEILRNHQ--KFHIASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLH 100
Cdd:pfam03859    1 KTRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIH 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30697970    101 CYYAHGEDNENFQRRCYWMLEQDLmHIVFVHYLEV 135
Cdd:pfam03859   81 CYYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
655-755 3.92e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  655 PNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADpspehpLG 734
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN------DG 219

                         90       100
                 ....*....|....*....|.
gi 30697970  735 KTAADLAYGNGHRGISGFLAE 755
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLE 240
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 893-914 3.30e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 38.85  E-value: 3.30e-04
                            10        20
                    ....*....|....*....|..
gi 30697970     893 IRQRIVKIQAHVRGHQVRKQYR 914
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 23-135 3.61e-71

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: 231.39  E-value: 3.61e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970     23 QHRWLRPAEICEILRNHQ--KFHIASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLH 100
Cdd:pfam03859    1 KTRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIH 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30697970    101 CYYAHGEDNENFQRRCYWMLEQDLmHIVFVHYLEV 135
Cdd:pfam03859   81 CYYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
 19-136 4.22e-67

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: 220.35  E-value: 4.22e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970      19 LSEAQHRWLRPAEICEILRNHQKFH--IASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSI 96
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTewLTTSPPTRPKSGSLFLFNRKKLKYFRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 30697970      97 DVLHCYYAHGEDNENFQRRCYWMLeqDLMHIVFVHYLEVK 136
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLL--QNPDIVLVHYLNVP 118
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
655-755 3.92e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  655 PNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADpspehpLG 734
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN------DG 219

                         90       100
                 ....*....|....*....|.
gi 30697970  735 KTAADLAYGNGHRGISGFLAE 755
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
641-720 6.96e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970    641 YLWLIHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIKpILAAGVSINFRDaNGWSALHWAAFSGREDTVAVLVSLGAD 720
Cdd:pfam12796    9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
 645-754 1.77e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970   645 IHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIK--PILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAG 722
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                          90       100       110
                  ....*....|....*....|....*....|...
gi 30697970   723 ALAdpspehPLGKTAADLAYGNGH-RGISGFLA 754
Cdd:PHA03095  285 AVS------SDGNTPLSLMVRNNNgRAVRAALA 311
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 893-914 3.30e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 38.85  E-value: 3.30e-04
                            10        20
                    ....*....|....*....|..
gi 30697970     893 IRQRIVKIQAHVRGHQVRKQYR 914
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 894-914 4.61e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.07  E-value: 4.61e-04
                           10        20
                   ....*....|....*....|.
gi 30697970    894 RQRIVKIQAHVRGHQVRKQYR 914
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 894-917 2.68e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.41  E-value: 2.68e-03
                         10        20
                 ....*....|....*....|....
gi 30697970  894 RQRIVKIQAHVRGHQVRKQYRAII 917
Cdd:cd21759   45 REALIKIQKTVRGYLARKKHRPRI 68
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 694-720 3.32e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.32e-03
                            10        20
                    ....*....|....*....|....*..
gi 30697970     694 NGWSALHWAAFSGREDTVAVLVSLGAD 720
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 23-135 3.61e-71

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: 231.39  E-value: 3.61e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970     23 QHRWLRPAEICEILRNHQ--KFHIASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLH 100
Cdd:pfam03859    1 KTRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIH 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30697970    101 CYYAHGEDNENFQRRCYWMLEQDLmHIVFVHYLEV 135
Cdd:pfam03859   81 CYYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
 19-136 4.22e-67

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: 220.35  E-value: 4.22e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970      19 LSEAQHRWLRPAEICEILRNHQKFH--IASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSI 96
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTewLTTSPPTRPKSGSLFLFNRKKLKYFRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 30697970      97 DVLHCYYAHGEDNENFQRRCYWMLeqDLMHIVFVHYLEVK 136
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLL--QNPDIVLVHYLNVP 118
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
655-755 3.92e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  655 PNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADpspehpLG 734
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN------DG 219

                         90       100
                 ....*....|....*....|.
gi 30697970  735 KTAADLAYGNGHRGISGFLAE 755
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-749 9.51e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.15  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  650 EEGKGPNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADpsp 729
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--- 184

                         90       100
                 ....*....|....*....|
gi 30697970  730 ehpLGKTAADLAYGNGHRGI 749
Cdd:COG0666  185 ---DGETPLHLAAENGHLEI 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
587-755 2.63e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  587 HHIFENVGEKRRKISKIMLLKDEKEPPLPGTIEKDLTELEAKERLIREEFEDKLYLWLIHKVTEEGKGPNILDEDGQGVL 666
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  667 HLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGadagalADPSPEHPLGKTAADLAYGNGH 746
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------ADVNAQDNDGNTPLHLAAANGN 165


                 ....*....
gi 30697970  747 RGISGFLAE 755
Cdd:COG0666  166 LEIVKLLLE 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
641-720 6.96e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970    641 YLWLIHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIKpILAAGVSINFRDaNGWSALHWAAFSGREDTVAVLVSLGAD 720
Cdd:pfam12796    9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
655-758 6.68e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 6.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970  655 PNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADPspehplG 734
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD------G 252

                         90       100
                 ....*....|....*....|....
gi 30697970  735 KTAADLAYGNGHRGISGFLAESSL 758
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
666-756 2.67e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970    666 LHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSlGADAGALADpspehplGKTAADLAYGNG 745
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-------GRTALHYAARSG 72

                           90
                   ....*....|.
gi 30697970    746 HRGISGFLAES 756
Cdd:pfam12796   73 HLEIVKLLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
 645-754 1.77e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970   645 IHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIK--PILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAG 722
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                          90       100       110
                  ....*....|....*....|....*....|...
gi 30697970   723 ALAdpspehPLGKTAADLAYGNGH-RGISGFLA 754
Cdd:PHA03095  285 AVS------SDGNTPLSLMVRNNNgRAVRAALA 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
665-715 2.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 30697970    665 VLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLV 715
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 644-711 2.07e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 2.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697970   644 LIHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALhWAAFSGREDTV 711
Cdd:PLN03192  540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKI 606
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 649-813 2.72e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970   649 TEEGKGPNILDEDGQGVLHLAAAlGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADPs 728
Cdd:PTZ00322   70 TEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697970   729 pehplGKTAADLAYGNGHRGISGFLAESSLTSYlekltvDAKENSSADS-SGAKAVLTVAERTATPMSYGDVPEtlSMKD 807
Cdd:PTZ00322  148 -----GKTPLELAEENGFREVVQLLSRHSQCHF------ELGANAKPDSfTGKPPSLEDSPISSHHPDFSAVPQ--PMMG 214


                  ....*.
gi 30697970   808 SLTAVL 813
Cdd:PTZ00322  215 SLIVIM 220
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 893-914 3.30e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 38.85  E-value: 3.30e-04
                            10        20
                    ....*....|....*....|..
gi 30697970     893 IRQRIVKIQAHVRGHQVRKQYR 914
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 894-914 4.61e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.07  E-value: 4.61e-04
                           10        20
                   ....*....|....*....|.
gi 30697970    894 RQRIVKIQAHVRGHQVRKQYR 914
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 894-917 2.68e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.41  E-value: 2.68e-03
                         10        20
                 ....*....|....*....|....
gi 30697970  894 RQRIVKIQAHVRGHQVRKQYRAII 917
Cdd:cd21759   45 REALIKIQKTVRGYLARKKHRPRI 68
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 694-720 3.32e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.32e-03
                            10        20
                    ....*....|....*....|....*..
gi 30697970     694 NGWSALHWAAFSGREDTVAVLVSLGAD 720
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
655-726 4.17e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 4.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697970  655 PNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALAD 726
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 694-720 6.59e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.59e-03
                           10        20
                   ....*....|....*....|....*...
gi 30697970    694 NGWSALHWAAFS-GREDTVAVLVSLGAD 720
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
695-753 7.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 7.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 30697970    695 GWSALHWAAFSGREDTVAVLVSLGADAGALADpspehpLGKTAADLAYGNGHRGISGFL 753
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG------NGETALHFAASNGNVEVLKLL 53
 
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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