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Conserved domains on  [gi|1907183189|ref|XP_036009205|]
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alpha-actinin-4 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 579-645 3.62e-31

Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition.


:

Pssm-ID: 430177  Cd Length: 69  Bit Score: 115.87  E-value: 3.62e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183189 579 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAAPGALDYKSFSTALYG 645
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-383 2.35e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 157 LAEKFRQKASIHEAWTDGKEAMLKQRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 236
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 237 RCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 316
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183189 317 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 383
Cdd:cd00176   152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 275-497 5.68e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 5.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 275 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 354
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 355 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRqfasqanmVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 433
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907183189 434 KQYERSIVDYKPSLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 497
Cdd:cd00176   149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 39-260 2.75e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  39 EDYERLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 115
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 116 MPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKQRDYETaTLSDIKAL 195
Cdd:cd00176    74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907183189 196 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALE 260
Cdd:cd00176   145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
PTZ00184 super family cl33172
calmodulin; Provisional
 502-606 8.80e-14

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 69.02  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 502 AKGISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTD 581
Cdd:PTZ00184    2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                          90       100
                  ....*....|....*....|....*.
gi 1907183189 582 TADQVIASFKVLAGDKN-FITAEELR 606
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNgFISAAELR 107
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1-21 4.95e-05

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


The actual alignment was detected with superfamily member cd21289:

Pssm-ID: 469584  Cd Length: 124  Bit Score: 43.17  E-value: 4.95e-05
                          10        20
                  ....*....|....*....|.
gi 1907183189   1 MTYVSCFYHAFSGAQKAETAA 21
Cdd:cd21289   104 MTYVSCFYHAFAGAEQAETAA 124
 
Name Accession Description Interval E-value
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 579-645 3.62e-31

Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition.


Pssm-ID: 430177  Cd Length: 69  Bit Score: 115.87  E-value: 3.62e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183189 579 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAAPGALDYKSFSTALYG 645
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-383 2.35e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 157 LAEKFRQKASIHEAWTDGKEAMLKQRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 236
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 237 RCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 316
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183189 317 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 383
Cdd:cd00176   152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 156-260 2.58e-21

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 89.30  E-value: 2.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 156 HLAEKFRQKASIHEAWTDGKEAMLKQRDYETaTLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVN 235
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*
gi 1907183189 236 TRCQKICDQWDNLGSLTHSRREALE 260
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
159-260 1.42e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.53  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  159 EKFRQKASIHEAWTDGKEAMLKQRDYeTATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRC 238
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 1907183189  239 QKICDQWDNLGSLTHSRREALE 260
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 275-497 5.68e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 5.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 275 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 354
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 355 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRqfasqanmVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 433
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907183189 434 KQYERSIVDYKPSLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 497
Cdd:cd00176   149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 39-260 2.75e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  39 EDYERLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 115
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 116 MPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKQRDYETaTLSDIKAL 195
Cdd:cd00176    74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907183189 196 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALE 260
Cdd:cd00176   145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
PTZ00184 PTZ00184
calmodulin; Provisional
 502-606 8.80e-14

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 69.02  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 502 AKGISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTD 581
Cdd:PTZ00184    2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                          90       100
                  ....*....|....*....|....*.
gi 1907183189 582 TADQVIASFKVLAGDKN-FITAEELR 606
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNgFISAAELR 107
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 512-574 1.49e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 62.95  E-value: 1.49e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907183189 512 EFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMS 574
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 36-146 2.49e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 57.71  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  36 HLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYrrvHKPPKVQEKCQLEInfNTLQTKLrLSNRPAF 115
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKAL---EAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907183189 116 MPSEGRMVSDINNGWQHLEQAEKGYEEWLLN 146
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 392-495 1.05e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.09  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 392 HLRRQFASQANMVGPWIQTKMEEIGRISI-EMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALIFDNKHTNY 470
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYgKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 1907183189 471 TMEHIRVGWEQLLTTIARTINEVEN 495
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 1-21 4.95e-05

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 43.17  E-value: 4.95e-05
                          10        20
                  ....*....|....*....|.
gi 1907183189   1 MTYVSCFYHAFSGAQKAETAA 21
Cdd:cd21289   104 MTYVSCFYHAFAGAEQAETAA 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
508-621 1.26e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 508 EQMQEFRASFNHFDKKQTGSMDSDDFRAllistgysLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADqVI 587
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-AR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907183189 588 ASFKVLAGDKN-FITAEELRR-----ELPPDQAEYCIARM 621
Cdd:COG5126    73 AAFDLLDTDGDgKISADEFRRlltalGVSEEEADELFARL 112
 
Name Accession Description Interval E-value
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 579-645 3.62e-31

Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition.


Pssm-ID: 430177  Cd Length: 69  Bit Score: 115.87  E-value: 3.62e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183189 579 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAAPGALDYKSFSTALYG 645
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-383 2.35e-29

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 115.62  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 157 LAEKFRQKASIHEAWTDGKEAMLKQRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 236
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 237 RCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 316
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183189 317 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 383
Cdd:cd00176   152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 156-260 2.58e-21

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 89.30  E-value: 2.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 156 HLAEKFRQKASIHEAWTDGKEAMLKQRDYETaTLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVN 235
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*
gi 1907183189 236 TRCQKICDQWDNLGSLTHSRREALE 260
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
159-260 1.42e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.53  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  159 EKFRQKASIHEAWTDGKEAMLKQRDYeTATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRC 238
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 1907183189  239 QKICDQWDNLGSLTHSRREALE 260
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 275-497 5.68e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 5.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 275 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 354
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 355 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRqfasqanmVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 433
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907183189 434 KQYERSIVDYKPSLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 497
Cdd:cd00176   149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 39-260 2.75e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  39 EDYERLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 115
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 116 MPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKQRDYETaTLSDIKAL 195
Cdd:cd00176    74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907183189 196 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALE 260
Cdd:cd00176   145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
PTZ00184 PTZ00184
calmodulin; Provisional
 502-606 8.80e-14

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 69.02  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 502 AKGISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTD 581
Cdd:PTZ00184    2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                          90       100
                  ....*....|....*....|....*.
gi 1907183189 582 TADQVIASFKVLAGDKN-FITAEELR 606
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNgFISAAELR 107
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 271-382 2.50e-13

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 66.57  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 271 QLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIhkeAQRIAESNHiklsG 350
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNEL---AEKLIDEGH----Y 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907183189 351 SNPYTTVTPQIINSKWEKVQQLVPKRDHALLE 382
Cdd:pfam00435  74 ASEEIQERLEELNERWEQLLELAAERKQKLEE 105
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 512-574 1.49e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 62.95  E-value: 1.49e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907183189 512 EFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMS 574
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 36-146 2.49e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 57.71  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  36 HLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYrrvHKPPKVQEKCQLEInfNTLQTKLrLSNRPAF 115
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKAL---EAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907183189 116 MPSEGRMVSDINNGWQHLEQAEKGYEEWLLN 146
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 392-495 1.05e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.09  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 392 HLRRQFASQANMVGPWIQTKMEEIGRISI-EMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALIFDNKHTNY 470
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYgKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 1907183189 471 TMEHIRVGWEQLLTTIARTINEVEN 495
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
PTZ00183 PTZ00183
centrin; Provisional
 504-607 5.12e-08

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 52.77  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 504 GISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTA 583
Cdd:PTZ00183   10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPR 89

                          90       100
                  ....*....|....*....|....*
gi 1907183189 584 DQVIASFKVLAGDKN-FITAEELRR 607
Cdd:PTZ00183   90 EEILKAFRLFDDDKTgKISLKNLKR 114
SPEC smart00150
Spectrin repeats;
275-380 1.57e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.64  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  275 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 354
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAEL---EAHEERVEALNELGEQLIEEGH----PDAEE 74

                           90       100
                   ....*....|....*....|....*.
gi 1907183189  355 TTVTPQIINSKWEKVQQLVPKRDHAL 380
Cdd:smart00150  75 IEERLEELNERWEELKELAEERRQKL 100
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 508-572 4.00e-05

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 44.51  E-value: 4.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183189 508 EQMQEF----RASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDF 572
Cdd:cd16185    59 AALHQFlsnmQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIEL 127
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 511-570 4.19e-05

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 44.44  E-value: 4.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 511 QEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFI 570
Cdd:cd16180    67 QDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFV 126
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 1-21 4.95e-05

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 43.17  E-value: 4.95e-05
                          10        20
                  ....*....|....*....|.
gi 1907183189   1 MTYVSCFYHAFSGAQKAETAA 21
Cdd:cd21289   104 MTYVSCFYHAFAGAEQAETAA 124
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 1-21 7.12e-05

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409137  Cd Length: 124  Bit Score: 42.75  E-value: 7.12e-05
                          10        20
                  ....*....|....*....|.
gi 1907183189   1 MTYVSCFYHAFSGAQKAETAA 21
Cdd:cd21288   104 MTYVSCFYHAFAGAEQAETAA 124
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 30-442 8.75e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189   30 VNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVP--QKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKL 107
Cdd:pfam15921   79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIdlQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAK 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  108 RLSNRpafmpsegrMVSDINNGWQHLEQAEKGYEEwLLNEIRRLerLDHLAEKFRQKASIHEAWT--------DGKEAML 179
Cdd:pfam15921  159 CLKED---------MLEDSNTQIEQLRKMMLSHEG-VLQEIRSI--LVDFEEASGKKIYEHDSMStmhfrslgSAISKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  180 KQRDYETATLSD-IKALIRKHEAFESD--------LAAHQDRVEQ-IAAIAQELNELDYYDS------HNVNTRCQKICD 243
Cdd:pfam15921  227 RELDTEISYLKGrIFPVEDQLEALKSEsqnkiellLQQHQDRIEQlISEHEVEITGLTEKASsarsqaNSIQSQLEIIQE 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  244 QWDNLGSLTHSRREALEKTEKQLETidqlHLEYAKRAapfnnwMESAMEDLQDMFIVHTIEEIEGLiSAHDQFKSTLPDA 323
Cdd:pfam15921  307 QARNQNSMYMRQLSDLESTVSQLRS----ELREAKRM------YEDKIEELEKQLVLANSELTEAR-TERDQFSQESGNL 375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189  324 DREREAILA-IHKEAQRIA---ESNHiKLSGSNPYTTVTPQIINSKWEKVQQLVpKRDHALLEEQsKQQSNEHLRRQFAS 399
Cdd:pfam15921  376 DDQLQKLLAdLHKREKELSlekEQNK-RLWDRDTGNSITIDHLRRELDDRNMEV-QRLEALLKAM-KSECQGQMERQMAA 452

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1907183189  400 qanmvgpwIQTKMEEIGRISiemngTLEDQLSHLKQYERSIVD 442
Cdd:pfam15921  453 --------IQGKNESLEKVS-----SLTAQLESTKEMLRKVVE 482
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
508-621 1.26e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 508 EQMQEFRASFNHFDKKQTGSMDSDDFRAllistgysLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADqVI 587
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-AR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907183189 588 ASFKVLAGDKN-FITAEELRR-----ELPPDQAEYCIARM 621
Cdd:COG5126    73 AAFDLLDTDGDgKISADEFRRlltalGVSEEEADELFARL 112
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 517-623 1.71e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 41.88  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 517 FNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETtdtdTADQVIASFKVLAG- 595
Cdd:cd15898     6 WIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT----ERPELEPIFKKYAGt 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907183189 596 DKNFITAEELRR--------ELPPDQAEYCIARMAP 623
Cdd:cd15898    82 NRDYMTLEEFIRflreeqgeNVSEEECEELIEKYEP 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
505-629 4.70e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 505 ISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTAD 584
Cdd:COG5126    27 FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907183189 585 QVIASFkvlagDKN---FITAEELRrelppdqaeyciARMAPYQGPDA 629
Cdd:COG5126   107 ELFARL-----DTDgdgKISFEEFV------------AAVRDYYTPDA 137
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 517-591 5.85e-04

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 41.03  E-value: 5.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907183189 517 FNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIM---SvvdpNHSGLVTFQAFIDFMSRETTdtdtadqVIASFK 591
Cdd:cd16196    77 FKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVlryS----NKDGRISFDDFIMCAVKLKT-------MFEIFK 143
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 511-575 4.18e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 38.36  E-value: 4.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 511 QEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGdaefNRIMSVV-----DPNhsGLVTFQAFIDFMSR 575
Cdd:cd16182    72 KKWQAIFKKFDTDRSGTLSSYELRKALESAGFHLS----NKVLQALvlryaDST--GRITFEDFVSCLVR 135
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 511-570 5.39e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 38.00  E-value: 5.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183189 511 QEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDAEFNRIMSVVDPNHSGLVTFQAFI 570
Cdd:cd16183    67 TDWQNCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFI 126
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 509-575 5.68e-03

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 37.95  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183189 509 QMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGDaEFNRIMSVVDPNHSGLVTFQAFIDFMSR 575
Cdd:cd16195    71 KLRKYKDIFQKADVSKSGFLSLSELRNAIQAAGIRVSD-DLLNLMALRYGDSSGRISFESFICLMLR 136
 
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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