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Conserved domains on  [gi|295393786|gb|ADG03678|]
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alpha actinin 4 short isoform [Homo sapiens]

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 ...
 622-688 1.13e-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: 117.41  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295393786  622 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAVPGALDYKSFSTALYG 688
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 195-421 2.77e-28

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: 112.92  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 195 LAEKFRQKASIHEAWTDGKEAMLKHRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 274
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 275 RCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 354
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295393786 355 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 421
Cdd:cd00176  152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 313-535 2.19e-15

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: 75.56  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 313 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 392
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 393 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQqsnehlrrQFASQANVVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 471
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295393786 472 KQYERSIVDYKPNLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 535
Cdd:cd00176  149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PTZ00184 super family cl33172
calmodulin; Provisional
 540-649 3.06e-14

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 70.56  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 540 AKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDvendrQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRE 619
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN-----PTEAELQDMINEVDADGNGTIDFPEFLTLMARK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 295393786 620 TTDTDTADQVIASFKVLAGDKN-FITAEELR 649
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 77-298 4.50e-13

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: 69.01  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  77 EDYEKLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 153
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 154 MPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKHRDYETaTLSDIKAL 233
Cdd:cd00176   74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295393786 234 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALE 298
Cdd:cd00176  145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
 
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 ...
 622-688 1.13e-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: 117.41  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295393786  622 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAVPGALDYKSFSTALYG 688
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 195-421 2.77e-28

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: 112.92  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 195 LAEKFRQKASIHEAWTDGKEAMLKHRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 274
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 275 RCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 354
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295393786 355 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 421
Cdd:cd00176  152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 194-298 2.75e-20

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: 86.22  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  194 HLAEKFRQKASIHEAWTDGKEAMLKHRDYETaTLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVN 273
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*
gi 295393786  274 TRCQKICDQWDALGSLTHSRREALE 298
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
197-298 3.65e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 77.37  E-value: 3.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786   197 EKFRQKASIHEAWTDGKEAMLKHRDYeTATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRC 276
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 295393786   277 QKICDQWDALGSLTHSRREALE 298
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 313-535 2.19e-15

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: 75.56  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 313 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 392
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 393 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQqsnehlrrQFASQANVVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 471
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295393786 472 KQYERSIVDYKPNLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 535
Cdd:cd00176  149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PTZ00184 PTZ00184
calmodulin; Provisional
 540-649 3.06e-14

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 70.56  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 540 AKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDvendrQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRE 619
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN-----PTEAELQDMINEVDADGNGTIDFPEFLTLMARK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 295393786 620 TTDTDTADQVIASFKVLAGDKN-FITAEELR 649
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 77-298 4.50e-13

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: 69.01  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  77 EDYEKLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 153
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 154 MPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKHRDYETaTLSDIKAL 233
Cdd:cd00176   74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295393786 234 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALE 298
Cdd:cd00176  145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 550-617 7.08e-13

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: 63.72  E-value: 7.08e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295393786 550 EFRASFNHFDKDHGGALGPEEFKACLISLGydvenDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMS 617
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-----EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 74-184 6.94e-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: 56.56  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786   74 HLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYrrvHKPPKVQEKCQLEInfNTLQTKLrLSNRPAF 153
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKAL---EAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 295393786  154 MPSEGKMVSDINNGWQHLEQAEKGYEEWLLN 184
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 430-533 7.60e-09

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: 53.86  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  430 HLRRQFASQANVVGPWIQTKMEEIGRISI-EMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNY 508
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYgKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 295393786  509 TMEHIRVGWEQLLTTIARTINEVEN 533
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
EF-hand_7 pfam13499
EF-hand domain pair;
548-617 9.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 9.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  548 MQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQgeaEFNRIMSLVDPNHSGLVTFQAFIDFMS 617
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDE---EVEELFKEFDLDKDGRISFEEFLELYS 67
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
458-652 1.54e-05

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.01  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 458 IEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEalIFDNKHTNYTMEHIRVGWEQLLTTIArtINEVENQILT 537
Cdd:COG5069  398 TNLFGDLRDQLILLQALSKKLMPMTVTHKLVKKQPASGIE--ENRFKAFENENYAVDLGITEGFSLVG--IKGLEILDGI 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 538 RDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQgeaefnrIMSLVDPNHS-GLVTFQAFIDFM 616
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEG-------IRSFGDPAGSvSGVFYLDVLKGI 546

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 295393786 617 SRETTDTDTADQVIASFKVLAGDKNFITAEELRREL 652
Cdd:COG5069  547 HSELVDYDLVTRGFTEFDDIADARSLAISSKILRSL 582
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
146-316 2.66e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 146 RLSNrpafmpSEgKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQ-KASIHEAWTDGKEAMLKHRDYET 224
Cdd:COG0497  217 RLSN------AE-KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAElAERLESALIELEEAASELRRYLD 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 225 AT-------------LSDIKALIRKHEAFESDLAAHQDRveqiaaIAQELNELDYYDSH--NVNTRCQKICDQWDALGS- 288
Cdd:COG0497  290 SLefdperleeveerLALLRRLARKYGVTVEELLAYAEE------LRAELAELENSDERleELEAELAEAEAELLEAAEk 363

                        170       180
                 ....*....|....*....|....*....
gi 295393786 289 LTHSRREALEKTEKQLEA-IDQLHLEYAK 316
Cdd:COG0497  364 LSAARKKAAKKLEKAVTAeLADLGMPNAR 392
 
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 ...
 622-688 1.13e-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: 117.41  E-value: 1.13e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295393786  622 DTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGP--DAVPGALDYKSFSTALYG 688
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 195-421 2.77e-28

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: 112.92  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 195 LAEKFRQKASIHEAWTDGKEAMLKHRDYEtATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNT 274
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 275 RCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLeyakraapFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQF 354
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295393786 355 KSTLPDADREREAILaihKEAQRIAESNHiklSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE 421
Cdd:cd00176  152 EEELEAHEPRLKSLN---ELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 194-298 2.75e-20

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: 86.22  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  194 HLAEKFRQKASIHEAWTDGKEAMLKHRDYETaTLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVN 273
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*
gi 295393786  274 TRCQKICDQWDALGSLTHSRREALE 298
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
197-298 3.65e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 77.37  E-value: 3.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786   197 EKFRQKASIHEAWTDGKEAMLKHRDYeTATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRC 276
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 295393786   277 QKICDQWDALGSLTHSRREALE 298
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 313-535 2.19e-15

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: 75.56  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 313 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 392
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL---AAHEERVEALNELGEQLIEEGH----PDAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 393 TTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQqsnehlrrQFASQANVVGPWIQTKMEEIGRISIEMN-GTLEDQLSHL 471
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295393786 472 KQYERSIVDYKPNLD-LLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQI 535
Cdd:cd00176  149 KELEEELEAHEPRLKsLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PTZ00184 PTZ00184
calmodulin; Provisional
 540-649 3.06e-14

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 70.56  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 540 AKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDvendrQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRE 619
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN-----PTEAELQDMINEVDADGNGTIDFPEFLTLMARK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 295393786 620 TTDTDTADQVIASFKVLAGDKN-FITAEELR 649
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 77-298 4.50e-13

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: 69.01  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  77 EDYEKLASDLLEWIRRTIPWLEDRVP---QKTIQEMQQKLEDFRDYRRVHKpPKVQEkcqleinFNTLQTKLRLSNRPAf 153
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYgddLESVEALLKKHEALEAELAAHE-ERVEA-------LNELGEQLIEEGHPD- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 154 MPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKfrqkasihEAWTDGKEAMLKHRDYETaTLSDIKAL 233
Cdd:cd00176   74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKEAALASEDLGK-DLESVEEL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295393786 234 IRKHEAFESDLAAHQDRVEQIAAIAQEL-NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALE 298
Cdd:cd00176  145 LKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 309-420 6.61e-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: 65.42  E-value: 6.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  309 QLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIhkeAQRIAESNHiklsG 388
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNEL---AEKLIDEGH----Y 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 295393786  389 SNPYTTVTPQIINSKWEKVQQLVPKRDHALLE 420
Cdd:pfam00435  74 ASEEIQERLEELNERWEQLLELAAERKQKLEE 105
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 550-617 7.08e-13

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: 63.72  E-value: 7.08e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295393786 550 EFRASFNHFDKDHGGALGPEEFKACLISLGydvenDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMS 617
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-----EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 74-184 6.94e-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: 56.56  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786   74 HLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYrrvHKPPKVQEKCQLEInfNTLQTKLrLSNRPAF 153
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKAL---EAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 295393786  154 MPSEGKMVSDINNGWQHLEQAEKGYEEWLLN 184
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
PTZ00183 PTZ00183
centrin; Provisional
 542-650 7.12e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 58.16  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 542 GISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDrqgeaEFNRIMSLVDPNHSGLVTFQAFIDFMSRETT 621
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKE-----EIKQMIADVDKDGSGKIDFEEFLDIMTKKLG 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 295393786 622 DTDTADQVIASFKVLAGDKN-FITAEELRR 650
Cdd:PTZ00183  85 ERDPREEILKAFRLFDDDKTgKISLKNLKR 114
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 430-533 7.60e-09

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: 53.86  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  430 HLRRQFASQANVVGPWIQTKMEEIGRISI-EMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNY 508
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYgKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 295393786  509 TMEHIRVGWEQLLTTIARTINEVEN 533
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
313-418 3.49e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786   313 EYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLpdaDREREAILAIHKEAQRIAESNHiklsGSNPY 392
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAEL---EAHEERVEALNELGEQLIEEGH----PDAEE 74

                           90       100
                   ....*....|....*....|....*.
gi 295393786   393 TTVTPQIINSKWEKVQQLVPKRDHAL 418
Cdd:smart00150  75 IEERLEELNERWEELKELAEERRQKL 100
EF-hand_7 pfam13499
EF-hand domain pair;
548-617 9.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 9.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786  548 MQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQgeaEFNRIMSLVDPNHSGLVTFQAFIDFMS 617
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDE---EVEELFKEFDLDKDGRISFEEFLELYS 67
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
458-652 1.54e-05

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.01  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 458 IEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEalIFDNKHTNYTMEHIRVGWEQLLTTIArtINEVENQILT 537
Cdd:COG5069  398 TNLFGDLRDQLILLQALSKKLMPMTVTHKLVKKQPASGIE--ENRFKAFENENYAVDLGITEGFSLVG--IKGLEILDGI 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 538 RDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQgeaefnrIMSLVDPNHS-GLVTFQAFIDFM 616
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEG-------IRSFGDPAGSvSGVFYLDVLKGI 546

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 295393786 617 SRETTDTDTADQVIASFKVLAGDKNFITAEELRREL 652
Cdd:COG5069  547 HSELVDYDLVTRGFTEFDDIADARSLAISSKILRSL 582
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
546-664 1.60e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 546 EQMQEFRASFNHFDKDHGGALGPEEFKAClislgydvendrqGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDT 625
Cdd:COG5126    2 LQRRKLDRRFDLLDADGDGVLERDDFEAL-------------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVE 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 295393786 626 ADqVIASFKVLagDKN---FITAEELRR-----ELPPDQAEYCIARM 664
Cdd:COG5126   69 PF-ARAAFDLL--DTDgdgKISADEFRRlltalGVSEEEADELFARL 112
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
509-616 1.60e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 509 TMEHIRVGWEQLLTTIARTINEVENQILTRD------AKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDv 582
Cdd:COG5126   23 ERDDFEALFRRLWATLFSEADTDGDGRISREefvagmESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVS- 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 295393786 583 endrqgEAEFNRIMSLVDPNHSGLVTFQAFIDFM 616
Cdd:COG5126  102 ------EEEADELFARLDTDGDGKISFEEFVAAV 129
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 555-666 2.51e-03

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: 38.80  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 555 FNHFDKDHGGALGPEEFKACLISLGYDVEndrqgEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETtdtdTADQVIASFK 634
Cdd:cd15898    6 WIKADKDGDGKLSLKEIKKLLKRLNIRVS-----EKELKKLFKEVDTNGDGTLTFDEFEELYKSLT----ERPELEPIFK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 295393786 635 VLAG-DKNFITAEELRR--------ELPPDQAEYCIARMAP 666
Cdd:cd15898   77 KYAGtNRDYMTLEEFIRflreeqgeNVSEEECEELIEKYEP 117
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
146-316 2.66e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 146 RLSNrpafmpSEgKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQ-KASIHEAWTDGKEAMLKHRDYET 224
Cdd:COG0497  217 RLSN------AE-KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAElAERLESALIELEEAASELRRYLD 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295393786 225 AT-------------LSDIKALIRKHEAFESDLAAHQDRveqiaaIAQELNELDYYDSH--NVNTRCQKICDQWDALGS- 288
Cdd:COG0497  290 SLefdperleeveerLALLRRLARKYGVTVEELLAYAEE------LRAELAELENSDERleELEAELAEAEAELLEAAEk 363

                        170       180
                 ....*....|....*....|....*....
gi 295393786 289 LTHSRREALEKTEKQLEA-IDQLHLEYAK 316
Cdd:COG0497  364 LSAARKKAAKKLEKAVTAeLADLGMPNAR 392
EF-hand_6 pfam13405
EF-hand domain;
550-579 2.81e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 295393786  550 EFRASFNHFDKDHGGALGPEEFKACLISLG 579
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
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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