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Conserved domains on  [gi|922552215|ref|XP_013604099|]
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PREDICTED: calmodulin-binding transcription activator 5 isoform X1 [Brassica oleracea var. oleracea]

Protein Classification

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 ...
 34-145 1.98e-49

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: 170.14  E-value: 1.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215   34 TRWLRPNEIHALLSNHK--YFTINVKPVHLPKSGTIVFFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHV 111
Cdd:pfam03859   2 TRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIHC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 922552215  112 YYAHGDDNPTFVRRCYWLLDKSQeHIVLVHYRET 145
Cdd:pfam03859  82 YYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-670 2.24e-12

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 482 QVRLSHLLFTSSSKISVFSSRISPDNLLEAKKLASRTSHLLNSWAYLMKSIQANELPFDQARDHLFELTLKNRLK--EWL 559
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEivKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 560 LEKvIENRNTKeyDSKGLGVIHLCAVLGYTwSI---LLFSWANIslDFRDKHGWTALHWAAYYGREKMVAALLSAGARPN 636
Cdd:COG0666  107 LEA-GADVNAR--DKDGETPLHLAAYNGNL-EIvklLLEAGADV--NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        170       180       190
                 ....*....|....*....|....*....|....
gi 922552215 637 LVTDptkeylGGCTAADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666  181 ARDN------DGETPLHLAAENGHLEIVKLLLEA 208
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
757-915 1.72e-05

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.92  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  757 AAMKIQHAFRNYETRRKIAAAARIQYMFQ----TWKMRREFlNMRKK---AIKIQAVFRGFQVRRQYQKITWSVGVLEKA 829
Cdd:COG5022   747 IATRIQRAIRGRYLRRRYLQALKRIKKIQviqhGFRLRRLV-DYELKwrlFIKLQPLLSLLGSRKEYRSYLACIIKLQKT 825

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  830 IlrwrlkrrgFRGLQVSQPEEKE----GTEAVEDFYKTSQKQAE-DRLERSVVRVQAMFRSKKAQQDYRRMKLAHEEAQL 904
Cdd:COG5022   826 I---------KREKKLRETEEVEfslkAEVLIQKFGRSLKAKKRfSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS 896

                         170
                  ....*....|.
gi 922552215  905 EYDGMQELDQM 915
Cdd:COG5022   897 LKLVNLELESE 907
 
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 ...
 34-145 1.98e-49

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: 170.14  E-value: 1.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215   34 TRWLRPNEIHALLSNHK--YFTINVKPVHLPKSGTIVFFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHV 111
Cdd:pfam03859   2 TRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIHC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 922552215  112 YYAHGDDNPTFVRRCYWLLDKSQeHIVLVHYRET 145
Cdd:pfam03859  82 YYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
 29-145 1.65e-47

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: 164.88  E-value: 1.65e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215    29 LEEAYTRWLRPNEIHALLSNHKYFT--INVKPVHLPKSGTIVFFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNE 106
Cdd:smart01076   1 LPEAKHRWLTPEEIAAILINFDKHTewLTTSPPTRPKSGSLFLFNRKKLKYFRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 922552215   107 ERIHVYYAHGDDNPTFVRRCYWLLDKsqEHIVLVHYRET 145
Cdd:smart01076  81 ECLHCYYAHSEINPTFHRRCYWLLQN--PDIVLVHYLNV 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-670 2.24e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 482 QVRLSHLLFTSSSKISVFSSRISPDNLLEAKKLASRTSHLLNSWAYLMKSIQANELPFDQARDHLFELTLKNRLK--EWL 559
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEivKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 560 LEKvIENRNTKeyDSKGLGVIHLCAVLGYTwSI---LLFSWANIslDFRDKHGWTALHWAAYYGREKMVAALLSAGARPN 636
Cdd:COG0666  107 LEA-GADVNAR--DKDGETPLHLAAYNGNL-EIvklLLEAGADV--NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        170       180       190
                 ....*....|....*....|....*....|....
gi 922552215 637 LVTDptkeylGGCTAADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666  181 ARDN------DGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
580-670 1.21e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  580 IHLCAVLGYTWSILLFSWANISLDFRDKHGWTALHWAAYYGREKMVAALLSaGARPNLVTDptkeylgGCTAADIAQQKG 659
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-------GRTALHYAARSG 72

                          90
                  ....*....|.
gi 922552215  660 YEGLAAFLAEK 670
Cdd:pfam12796  73 HLEIVKLLLEK 83
COG5022 COG5022
Myosin heavy chain [General function prediction only];
757-915 1.72e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.92  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  757 AAMKIQHAFRNYETRRKIAAAARIQYMFQ----TWKMRREFlNMRKK---AIKIQAVFRGFQVRRQYQKITWSVGVLEKA 829
Cdd:COG5022   747 IATRIQRAIRGRYLRRRYLQALKRIKKIQviqhGFRLRRLV-DYELKwrlFIKLQPLLSLLGSRKEYRSYLACIIKLQKT 825

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  830 IlrwrlkrrgFRGLQVSQPEEKE----GTEAVEDFYKTSQKQAE-DRLERSVVRVQAMFRSKKAQQDYRRMKLAHEEAQL 904
Cdd:COG5022   826 I---------KREKKLRETEEVEfslkAEVLIQKFGRSLKAKKRfSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS 896

                         170
                  ....*....|.
gi 922552215  905 EYDGMQELDQM 915
Cdd:COG5022   897 LKLVNLELESE 907
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 608-637 2.59e-05

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: 41.80  E-value: 2.59e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 922552215   608 HGWTALHWAAYYGREKMVAALLSAGARPNL 637
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 573-640 5.95e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 573 DSKGLGVIHLCAVLGYTWSILLFSW--ANISLDFRDKHGWTALHWAAYYGREKMVAALLSAGARPNLVTD 640
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRSLVLPLliAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 796-817 1.09e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 1.09e-04
                           10        20
                   ....*....|....*....|..
gi 922552215   796 MRKKAIKIQAVFRGFQVRRQYQ 817
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRYK 23
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 790-818 1.42e-04

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: 39.83  E-value: 1.42e-04
                         10        20
                 ....*....|....*....|....*....
gi 922552215 790 RREFLNMRKKAIKIQAVFRGFQVRRQYQK 818
Cdd:cd23767    2 EEELQRMNRAATLIQALWRGYKVRKELKK 30
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 797-817 3.78e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.45  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|.
gi 922552215  797 RKKAIKIQAVFRGFQVRRQYQ 817
Cdd:pfam00612   1 RKAAIKIQAAWRGYLARKRYK 21
 
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 ...
 34-145 1.98e-49

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: 170.14  E-value: 1.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215   34 TRWLRPNEIHALLSNHK--YFTINVKPVHLPKSGTIVFFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHV 111
Cdd:pfam03859   2 TRWLKPQEILAILLNYDpyGFCITPEPPPRPPSGSLFLFDRKKLRYFRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIHC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 922552215  112 YYAHGDDNPTFVRRCYWLLDKSQeHIVLVHYRET 145
Cdd:pfam03859  82 YYAHSEDNPTFQRRIYWLLDSDY-HIVLVHYLNV 114
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
 29-145 1.65e-47

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: 164.88  E-value: 1.65e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215    29 LEEAYTRWLRPNEIHALLSNHKYFT--INVKPVHLPKSGTIVFFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNE 106
Cdd:smart01076   1 LPEAKHRWLTPEEIAAILINFDKHTewLTTSPPTRPKSGSLFLFNRKKLKYFRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 922552215   107 ERIHVYYAHGDDNPTFVRRCYWLLDKsqEHIVLVHYRET 145
Cdd:smart01076  81 ECLHCYYAHSEINPTFHRRCYWLLQN--PDIVLVHYLNV 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-670 2.24e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 482 QVRLSHLLFTSSSKISVFSSRISPDNLLEAKKLASRTSHLLNSWAYLMKSIQANELPFDQARDHLFELTLKNRLK--EWL 559
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEivKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 560 LEKvIENRNTKeyDSKGLGVIHLCAVLGYTwSI---LLFSWANIslDFRDKHGWTALHWAAYYGREKMVAALLSAGARPN 636
Cdd:COG0666  107 LEA-GADVNAR--DKDGETPLHLAAYNGNL-EIvklLLEAGADV--NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        170       180       190
                 ....*....|....*....|....*....|....
gi 922552215 637 LVTDptkeylGGCTAADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666  181 ARDN------DGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
573-670 6.51e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 573 DSKGLGVIHLCAVLGYTWSI--LLFSWANIslDFRDKHGWTALHWAAYYGREKMVAALLSAGARPNLVTDptkeylGGCT 650
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVklLLEAGADV--NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN------DGKT 221

                         90       100
                 ....*....|....*....|
gi 922552215 651 AADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666  222 ALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
580-670 1.21e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  580 IHLCAVLGYTWSILLFSWANISLDFRDKHGWTALHWAAYYGREKMVAALLSaGARPNLVTDptkeylgGCTAADIAQQKG 659
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-------GRTALHYAARSG 72

                          90
                  ....*....|.
gi 922552215  660 YEGLAAFLAEK 670
Cdd:pfam12796  73 HLEIVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-670 4.19e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 528 LMKSIQANELPFDQARDHLFELTLKNRLKEWLLEKVIENRNTKEYDSKGLGVIHLCAVLGYTWSILLFSWANISLDFRDK 607
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922552215 608 HGWTALHWAAYYGREKMVAALLSAGARPNLVTDptkeylGGCTAADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDK------DGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
557-637 1.69e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  557 EWLLEKVIENRNTkeyDSKGLGVIHLCAVLGYTwSILLFSWANISLDFRDkHGWTALHWAAYYGREKMVAALLSAGARPN 636
Cdd:pfam12796  14 KLLLENGADANLQ---DKNGRTALHLAAKNGHL-EIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88


                  .
gi 922552215  637 L 637
Cdd:pfam12796  89 V 89
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 608-640 1.00e-05

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: 43.05  E-value: 1.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 922552215  608 HGWTALHWAAY-YGREKMVAALLSAGARPNLVTD 640
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
COG5022 COG5022
Myosin heavy chain [General function prediction only];
757-915 1.72e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.92  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  757 AAMKIQHAFRNYETRRKIAAAARIQYMFQ----TWKMRREFlNMRKK---AIKIQAVFRGFQVRRQYQKITWSVGVLEKA 829
Cdd:COG5022   747 IATRIQRAIRGRYLRRRYLQALKRIKKIQviqhGFRLRRLV-DYELKwrlFIKLQPLLSLLGSRKEYRSYLACIIKLQKT 825

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215  830 IlrwrlkrrgFRGLQVSQPEEKE----GTEAVEDFYKTSQKQAE-DRLERSVVRVQAMFRSKKAQQDYRRMKLAHEEAQL 904
Cdd:COG5022   826 I---------KREKKLRETEEVEfslkAEVLIQKFGRSLKAKKRfSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS 896

                         170
                  ....*....|.
gi 922552215  905 EYDGMQELDQM 915
Cdd:COG5022   897 LKLVNLELESE 907
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 608-637 2.59e-05

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: 41.80  E-value: 2.59e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 922552215   608 HGWTALHWAAYYGREKMVAALLSAGARPNL 637
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 573-640 5.95e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922552215 573 DSKGLGVIHLCAVLGYTWSILLFSW--ANISLDFRDKHGWTALHWAAYYGREKMVAALLSAGARPNLVTD 640
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRSLVLPLliAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
609-667 8.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 8.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922552215  609 GWTALHWAAYYGREKMVAALLSAGARPNLVTDptkeylGGCTAADIAQQKGYEGLAAFL 667
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG------NGETALHFAASNGNVEVLKLL 53
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 796-817 1.09e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 1.09e-04
                           10        20
                   ....*....|....*....|..
gi 922552215   796 MRKKAIKIQAVFRGFQVRRQYQ 817
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRYK 23
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 790-818 1.42e-04

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: 39.83  E-value: 1.42e-04
                         10        20
                 ....*....|....*....|....*....
gi 922552215 790 RREFLNMRKKAIKIQAVFRGFQVRRQYQK 818
Cdd:cd23767    2 EEELQRMNRAATLIQALWRGYKVRKELKK 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 608-636 3.07e-04

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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 3.07e-04
                          10        20
                  ....*....|....*....|....*....
gi 922552215  608 HGWTALHWAAYYGREKMVAALLSAGARPN 636
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 797-817 3.78e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.45  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|.
gi 922552215  797 RKKAIKIQAVFRGFQVRRQYQ 817
Cdd:pfam00612   1 RKAAIKIQAAWRGYLARKRYK 21
Ank_5 pfam13857
Ankyrin repeats (many copies);
599-655 1.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922552215  599 NISLDFRDKHGWTALHWAAYYGREKMVAALLSAGARPNLVTDptkeylGGCTAADIA 655
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE------EGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
576-629 1.43e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922552215  576 GLGVIHLCAVLGY--TWSILLFSWANISLdfRDKHGWTALHWAAYYGREKMVAALL 629
Cdd:pfam13637   1 ELTALHAAAASGHleLLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
598-670 1.94e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.09  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922552215 598 ANISLdfRDKHGWTALHWAAYYGREKMVAALLSAGARPNLVTDPTKEYLGGCTAADIAQQKGYEGLAAFLAEK 670
Cdd:COG0666  210 ADVNA--KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
 
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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