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Conserved domains on  [gi|34577049|ref|NP_056363|]
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dystonin isoform 1eA precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 4864-4942 1.25e-37

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


:

Pssm-ID: 128539  Cd Length: 73  Bit Score: 137.19  E-value: 1.25e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049    4864 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRAKG 4942
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3967-4182 9.91e-36

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: 137.19  E-value: 9.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3967 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 4046
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4047 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 4126
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 4127 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 4182
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
 651-728 6.01e-34

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


:

Pssm-ID: 465730  Cd Length: 78  Bit Score: 126.95  E-value: 6.01e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049    651 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 728
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4406-4618 2.29e-31

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: 124.48  E-value: 2.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4406 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4486 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 4565
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4566 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 4618
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4293-4509 1.15e-26

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: 111.00  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4293 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 4372
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4373 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 4452
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 4453 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 4509
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3859-4073 5.68e-23

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: 100.21  E-value: 5.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3859 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3939 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 4018
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 4019 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 4073
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3747-3964 7.84e-21

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: 94.05  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3747 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 3826
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3827 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 3906
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3907 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 3964
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
 550-616 1.21e-20

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.21e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049    550 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 616
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4075-4291 1.49e-20

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: 93.28  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4075 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 4154
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4155 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 4234
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 4235 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 4291
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 375-557 4.99e-19

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: 89.04  E-value: 4.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  375 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 454
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  455 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 534
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158

                        170       180
                 ....*....|....*....|...
gi 34577049  535 KSTIANLMGKAKTIIQLKPRNSD 557
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAD 181
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2870-3085 5.75e-17

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: 82.88  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2870 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 2949
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2950 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKVvKAQIQEQKLLQRL 3029
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 3030 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 3085
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3529-3745 7.51e-17

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: 82.49  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3529 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 3608
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3609 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 3688
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3689 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 3745
Cdd:cd00176  161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2984-3197 1.82e-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: 81.34  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2984 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 3063
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3064 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHN 3143
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34577049 3144 KHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHSRSELLQQAL 3197
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3419-3632 2.72e-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: 80.95  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3419 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 3498
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3499 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 3578
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 3579 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 3632
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2102-2323 8.79e-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: 79.41  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2102 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 2181
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2182 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 2261
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2262 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 2323
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2328-2542 6.37e-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: 77.10  E-value: 6.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2328 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 2405
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2406 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 2485
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 2486 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 2542
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3091-3306 1.79e-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: 72.86  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3091 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLkVLSSREDKDMVQS 3170
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3171 KLDFSQVWYIEIQEKSHSRSELLQQALCNAKIFgEDEVELMNWLNEvhdKLSKLSVQDY--STEGLWKQQSELRVLQEDI 3248
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEE---KEAALASEDLgkDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3249 LLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 3306
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1512-1741 2.72e-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: 72.09  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1512 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 1591
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1592 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 1671
Cdd:cd00176   76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1672 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 1741
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3308-3523 1.50e-12

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: 70.17  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3308 LARRLHSTHEELCTWLDKVEVELLSyeTQVLKGEEASQAQMRP-KELKKEAKNNKALLDSLNEVSSALLELVPWRAREgL 3386
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKhEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3387 EKMVAEDNERYRLVSDTITQKVEEIDAAiLRSQQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEI 3466
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3467 LRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERA 3523
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4789-4851 1.48e-10

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: 59.87  E-value: 1.48e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALH 4851
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1185-1983 5.57e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 5.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1185 RNELEKQVKTLQ------ESYNLLfSESLKQLQESQTSGDVKVEEKIVAERQQEYKEkLQGICDLLTQTENRLIGHQEAF 1258
Cdd:TIGR02168  195 LNELERQLKSLErqaekaERYKEL-KAELRELELALLVLRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1259 MIGDGTVElKKYQSKQEELQ------KDMQGSAQALAEVVKNTENFLKENGEKL---------SQEDKALIEQKLNEAKI 1323
Cdd:TIGR02168  273 RLEVSELE-EEIEELQKELYalaneiSRLEQQKQILRERLANLERQLEELEAQLeeleskldeLAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1324 KCEQLNLK---AEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQ 1400
Cdd:TIGR02168  352 ELESLEAEleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1401 EGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEK 1480
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQ------EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEG 503

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1481 LQKNMKELKvhyetalaESEKKMKLTHSLQEELEKFDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSF 1557
Cdd:TIGR02168  504 FSEGVKALL--------KNQSGLSGILGVLSELISVDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTF 575

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1558 SE-DVISH---KGDLRYITISGNRVLEAAKSCSKRD-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkc 1620
Cdd:TIGR02168  576 LPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG-- 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1621 nvlgnnlkDLVdkyqhyedASCGLLAGlqACEATASKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEV 1700
Cdd:TIGR02168  653 --------DLV--------RPGGVITG--GSAKTNSSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEE 709

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1701 LLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN---ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLN 1777
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLE----------------EA 773

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1778 STALQDIISKNIMLEQDIAGRQSSINAMNEKVkkfmettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVE 1857
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREAL------------DELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1858 LFENLSEKLQtfletktqaltevdvpgKDVTELSQYMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNL 1937
Cdd:TIGR02168  842 DLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEEL 899

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*.
gi 34577049   1938 SKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKV 1983
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2544-2755 1.13e-06

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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 52.83  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2544 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 2623
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2624 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 2703
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2704 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 2755
Cdd:cd00176  160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
282-373 1.65e-06

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.64  E-value: 1.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049     282 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 358
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86

                            90
                    ....*....|....*
gi 34577049     359 AKLLNTSRNQERHLD 373
Cdd:smart00150   87 EELKELAEERRQKLE 101
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 710-1517 3.46e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 50.74  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    710 QLEKEVNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKE 789
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    790 LERLKDDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQ----VYSMSSTYIDKLKTVNLVLKNTQAAEalvkLY 865
Cdd:pfam02463  281 KKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKkaekELKKEKEEIEELEKELKELEIKREAE----EE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    866 ETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVE-- 943
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEee 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    944 ---RWQNVHVQIDNRLRDLEGIGKSLKYYRDTyhPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQS 1020
Cdd:pfam02463  437 esiELKQGKLTEEKEELEKQELKLLKDELELK--KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1021 KM--------DECQKYAEQYSATVKDYELQTMTYRAMVDSQQKSPVKRRR------------MQSSADLIIQEFMDLRTR 1080
Cdd:pfam02463  515 LIkdgvggriISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQklvraltelplgARKLRLLIPKLKLPLKSI 594

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1081 YTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQ-KWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKK 1159
Cdd:pfam02463  595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1160 EQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLF----SESLKQLQESQTSGDVKVEEKIVAERQQEYkE 1235
Cdd:pfam02463  675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEaeelLADRVQEAQDKINEELKLLKQKIDEEEEEE-E 753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1236 KLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIE 1315
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1316 QKLNEAKIKCEQLNLKAE-QSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENlldwlsnvdKDSERAGTKHKQVIEQ 1394
Cdd:pfam02463  834 ELEELALELKEEQKLEKLaEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL---------ESKEEKEKEEKKELEE 904

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1395 NGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQvgttQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQgqyLS 1474
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEE----PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV---NL 977

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 34577049   1475 PEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFD 1517
Cdd:pfam02463  978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
 
Name Accession Description Interval E-value
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 4864-4942 1.25e-37

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 137.19  E-value: 1.25e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049    4864 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRAKG 4942
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3967-4182 9.91e-36

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: 137.19  E-value: 9.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3967 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 4046
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4047 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 4126
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 4127 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 4182
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 4866-4940 9.97e-35

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 128.87  E-value: 9.97e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34577049   4866 IEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRA 4940
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
 651-728 6.01e-34

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


Pssm-ID: 465730  Cd Length: 78  Bit Score: 126.95  E-value: 6.01e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049    651 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 728
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4406-4618 2.29e-31

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: 124.48  E-value: 2.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4406 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4486 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 4565
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4566 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 4618
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4293-4509 1.15e-26

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: 111.00  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4293 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 4372
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4373 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 4452
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 4453 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 4509
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3859-4073 5.68e-23

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: 100.21  E-value: 5.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3859 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3939 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 4018
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 4019 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 4073
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3747-3964 7.84e-21

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: 94.05  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3747 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 3826
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3827 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 3906
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3907 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 3964
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
 550-616 1.21e-20

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.21e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049    550 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 616
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4075-4291 1.49e-20

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: 93.28  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4075 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 4154
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4155 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 4234
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 4235 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 4291
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 375-557 4.99e-19

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: 89.04  E-value: 4.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  375 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 454
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  455 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 534
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158

                        170       180
                 ....*....|....*....|...
gi 34577049  535 KSTIANLMGKAKTIIQLKPRNSD 557
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAD 181
SPEC smart00150
Spectrin repeats;
3969-4070 3.12e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.07  E-value: 3.12e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3969 QFQHALDELLAWLTHTEGLLSeQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 4048
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    4049 EVLNQRWQNVLEKTEQRKQQLD 4070
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2870-3085 5.75e-17

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: 82.88  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2870 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 2949
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2950 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKVvKAQIQEQKLLQRL 3029
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 3030 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 3085
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3529-3745 7.51e-17

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: 82.49  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3529 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 3608
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3609 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 3688
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3689 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 3745
Cdd:cd00176  161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2984-3197 1.82e-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: 81.34  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2984 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 3063
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3064 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHN 3143
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34577049 3144 KHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHSRSELLQQAL 3197
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3419-3632 2.72e-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: 80.95  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3419 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 3498
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3499 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 3578
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 3579 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 3632
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2102-2323 8.79e-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: 79.41  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2102 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 2181
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2182 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 2261
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2262 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 2323
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2328-2542 6.37e-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: 77.10  E-value: 6.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2328 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 2405
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2406 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 2485
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 2486 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 2542
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3091-3306 1.79e-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: 72.86  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3091 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLkVLSSREDKDMVQS 3170
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3171 KLDFSQVWYIEIQEKSHSRSELLQQALCNAKIFgEDEVELMNWLNEvhdKLSKLSVQDY--STEGLWKQQSELRVLQEDI 3248
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEE---KEAALASEDLgkDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3249 LLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 3306
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3969-4069 2.07e-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: 69.27  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3969 QFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 4048
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82

                           90       100
                   ....*....|....*....|.
gi 34577049   4049 EVLNQRWQNVLEKTEQRKQQL 4069
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1512-1741 2.72e-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: 72.09  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1512 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 1591
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1592 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 1671
Cdd:cd00176   76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1672 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 1741
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
4406-4506 4.44e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.13  E-value: 4.44e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4406 QFTDALQALIDWLYRVEPQLAeDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049    4486 ELSTRWETVCALSISKQTRLE 4506
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3308-3523 1.50e-12

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: 70.17  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3308 LARRLHSTHEELCTWLDKVEVELLSyeTQVLKGEEASQAQMRP-KELKKEAKNNKALLDSLNEVSSALLELVPWRAREgL 3386
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKhEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3387 EKMVAEDNERYRLVSDTITQKVEEIDAAiLRSQQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEI 3466
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3467 LRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERA 3523
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
4296-4398 1.17e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 1.17e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4296 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSlaDDNLKLDDM 4375
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    4376 LSELRDKWDTICGKSVERQNKLE 4398
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4789-4851 1.48e-10

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: 59.87  E-value: 1.48e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALH 4851
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4789-4852 1.93e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 1.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEmsAVADIFDRDGDGYIDYYEFVAALHP 4852
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD--ELFARLDTDGDGKISFEEFVAAVRD 131
SPEC smart00150
Spectrin repeats;
376-476 4.46e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 4.46e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049     376 HNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRA 455
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049     456 AMQTQWSWILQLCQCVEQHIK 476
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1185-1983 5.57e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 5.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1185 RNELEKQVKTLQ------ESYNLLfSESLKQLQESQTSGDVKVEEKIVAERQQEYKEkLQGICDLLTQTENRLIGHQEAF 1258
Cdd:TIGR02168  195 LNELERQLKSLErqaekaERYKEL-KAELRELELALLVLRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1259 MIGDGTVElKKYQSKQEELQ------KDMQGSAQALAEVVKNTENFLKENGEKL---------SQEDKALIEQKLNEAKI 1323
Cdd:TIGR02168  273 RLEVSELE-EEIEELQKELYalaneiSRLEQQKQILRERLANLERQLEELEAQLeeleskldeLAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1324 KCEQLNLK---AEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQ 1400
Cdd:TIGR02168  352 ELESLEAEleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1401 EGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEK 1480
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQ------EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEG 503

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1481 LQKNMKELKvhyetalaESEKKMKLTHSLQEELEKFDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSF 1557
Cdd:TIGR02168  504 FSEGVKALL--------KNQSGLSGILGVLSELISVDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTF 575

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1558 SE-DVISH---KGDLRYITISGNRVLEAAKSCSKRD-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkc 1620
Cdd:TIGR02168  576 LPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG-- 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1621 nvlgnnlkDLVdkyqhyedASCGLLAGlqACEATASKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEV 1700
Cdd:TIGR02168  653 --------DLV--------RPGGVITG--GSAKTNSSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEE 709

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1701 LLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN---ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLN 1777
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLE----------------EA 773

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1778 STALQDIISKNIMLEQDIAGRQSSINAMNEKVkkfmettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVE 1857
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREAL------------DELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1858 LFENLSEKLQtfletktqaltevdvpgKDVTELSQYMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNL 1937
Cdd:TIGR02168  842 DLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEEL 899

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*.
gi 34577049   1938 SKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKV 1983
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2223-2432 2.26e-09

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: 60.92  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2223 AQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSrpgEDPSLRGIVKEQLAAVT 2302
Cdd:cd00176   10 DELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDAEEIQERLEELN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2303 QKWDSLTGQLSDRCDWIDQAIvkstQYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQ 2380
Cdd:cd00176   86 QRWEELRELAEERRQRLEEAL----DLQQFFRDADDLEQWLEEKEAalASEDLGKDLESVEELLKKHKELEEELEAHEPR 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2381 IKVAQALCEDLSALvKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSA 2432
Cdd:cd00176  162 LKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
2984-3085 1.13e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.80  E-value: 1.13e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2984 RFQDALESLLSWMVDTEELVAnQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 3063
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    3064 SLLDSRWEALLNKAETRNRQLE 3085
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
2104-2209 3.53e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.26  E-value: 3.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2104 QKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAPRW 2183
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEI 75

                            90       100
                    ....*....|....*....|....*.
gi 34577049    2184 KQMLTEIDSKWQELNQLTIDRQQKLE 2209
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
EF-hand_7 pfam13499
EF-hand domain pair;
4787-4850 6.28e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.26  E-value: 6.28e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049   4787 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 4850
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPEC smart00150
Spectrin repeats;
2437-2539 7.33e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 7.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2437 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 2516
Cdd:smart00150    1 QQFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQ-LIEEGHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    2517 LNTIKTNWDTFNKQVKERENKLK 2539
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3749-3851 8.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 8.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3749 EKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKS 3828
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3829 IDELNSAWDSLNKAWKDRIDKLE 3851
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2102-2210 1.57e-07

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: 52.71  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2102 KLQKAQEESSAMMQWLQKMNKTATkwqQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 2181
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASE 76

                           90       100
                   ....*....|....*....|....*....
gi 34577049   2182 RWKQMLTEIDSKWQELNQLTIDRQQKLEE 2210
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4187-4288 2.12e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 2.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4187 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIKNLL 4266
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    4267 ISVQSRWEKVVQRLVERGRSLD 4288
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3859-3961 2.78e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 2.78e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3859 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--IEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3939 LMELKLIWDSLEERIINRQHKLE 3961
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2333-3134 3.74e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2333 LRSLSDKLSDLDNKLSSSLAVSTHpDAMNQQLETAQKMKQEIQQEKKQIKVAQalcEDLSALVKEEYLKAELSRQLEGIL 2412
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2413 KSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKS-HPISAKLDVLeslikdhkdfsktltaqshmy 2491
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElAELEEKLEEL--------------------- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2492 eKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKF 2571
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2572 CLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANsllsvcEIDKEVvtDENKSLIQKVDMVTEQLHSKKFCLENMTQK 2651
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREEL--EEAEQALDAAERELAQLQARLDSLERLQEN 500

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2652 FKEFQEVSKEskrQLQCAKEQLDIHDSLGSQaysnkyltmLQTQQKSLQALkhQVDLAKRLaQDLVVEASDSkgtsdVLL 2731
Cdd:TIGR02168  501 LEGFSEGVKA---LLKNQSGLSGILGVLSEL---------ISVDEGYEAAI--EAALGGRL-QAVVVENLNA-----AKK 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2732 QVETIAQEHSTlsqqvdeKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAPVGRDA-----------ETLQk 2797
Cdd:TIGR02168  561 AIAFLKQNELG-------RVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLD- 632

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2798 qkeTIKAFLKKLEALM--------------ASNDNANKTCKMMLAT----EETSPDLVGIKRDLEALSKQCNKLLDRAQA 2859
Cdd:TIGR02168  633 ---NALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEE 709

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2860 REEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQ 2939
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2940 SAAK-STSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKA 3018
Cdd:TIGR02168  790 QIEQlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3019 QIQEQklLQRLLDDRKSTVEVIKREGEKIATTAEPADKVkiLKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETL 3098
Cdd:TIGR02168  870 ELESE--LEALLNERASLEEALALLRSELEELSEELREL--ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945

                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 34577049   3099 epLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHKA 3134
Cdd:TIGR02168  946 --SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3773-3852 4.96e-07

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: 51.17  E-value: 4.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3773 EDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEE 3852
Cdd:pfam00435   27 EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4296-4399 5.63e-07

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: 50.78  E-value: 5.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4296 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKLDDM 4375
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 34577049   4376 LSELRDKWDTICGKSVERQNKLEE 4399
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4406-4507 6.03e-07

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: 50.78  E-value: 6.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4406 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 34577049   4486 ELSTRWETVCALSISKQTRLEA 4507
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
3529-3629 8.45e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 8.45e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3529 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 3608
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049    3609 AADTLYSQIKEDVKKRAVALD 3629
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3419-3521 9.59e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 9.59e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3419 QQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTAcSEEEKQSMKKK 3498
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3499 LDKVLKNYDTICQINSERYLQLE 3521
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2544-2755 1.13e-06

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: 52.83  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2544 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 2623
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2624 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 2703
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2704 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 2755
Cdd:cd00176  160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
282-373 1.65e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.64  E-value: 1.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049     282 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 358
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86

                            90
                    ....*....|....*
gi 34577049     359 AKLLNTSRNQERHLD 373
Cdd:smart00150   87 EELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2437-2540 2.67e-06

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: 48.85  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2437 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 2516
Cdd:pfam00435    4 QQFFRDADDLESWIE-EKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEK-LIDEGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 34577049   2517 LNTIKTNWDTFNKQVKERENKLKE 2540
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1635-1741 4.88e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 4.88e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    1635 QHYEDASCGLLAGLQACEATASkhlSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKND 1714
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA---SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH---PDAEE 74

                            90       100
                    ....*....|....*....|....*..
gi 34577049    1715 IQKTLDDIVGRYEDLSKSVNERNEKLQ 1741
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3416-3522 1.02e-05

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: 47.31  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3416 LRSQQFDQAADAELSWITETEKKLMSlGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQsM 3495
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-I 78

                           90       100
                   ....*....|....*....|....*..
gi 34577049   3496 KKKLDKVLKNYDTICQINSERYLQLER 3522
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 710-1517 3.46e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.74  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    710 QLEKEVNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKE 789
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    790 LERLKDDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQ----VYSMSSTYIDKLKTVNLVLKNTQAAEalvkLY 865
Cdd:pfam02463  281 KKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKkaekELKKEKEEIEELEKELKELEIKREAE----EE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    866 ETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVE-- 943
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEee 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    944 ---RWQNVHVQIDNRLRDLEGIGKSLKYYRDTyhPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQS 1020
Cdd:pfam02463  437 esiELKQGKLTEEKEELEKQELKLLKDELELK--KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1021 KM--------DECQKYAEQYSATVKDYELQTMTYRAMVDSQQKSPVKRRR------------MQSSADLIIQEFMDLRTR 1080
Cdd:pfam02463  515 LIkdgvggriISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQklvraltelplgARKLRLLIPKLKLPLKSI 594

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1081 YTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQ-KWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKK 1159
Cdd:pfam02463  595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1160 EQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLF----SESLKQLQESQTSGDVKVEEKIVAERQQEYkE 1235
Cdd:pfam02463  675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEaeelLADRVQEAQDKINEELKLLKQKIDEEEEEE-E 753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1236 KLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIE 1315
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1316 QKLNEAKIKCEQLNLKAE-QSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENlldwlsnvdKDSERAGTKHKQVIEQ 1394
Cdd:pfam02463  834 ELEELALELKEEQKLEKLaEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL---------ESKEEKEKEEKKELEE 904

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1395 NGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQvgttQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQgqyLS 1474
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEE----PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV---NL 977

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 34577049   1475 PEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFD 1517
Cdd:pfam02463  978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2984-3085 4.19e-05

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: 45.77  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2984 RFQDALESLLSWMVDTEELVANQKPPSaEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 3063
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|..
gi 34577049   3064 SLLDSRWEALLNKAETRNRQLE 3085
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1203-1989 8.09e-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: 49.35  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1203 FSESLKQLQESQTsgdvkvEEKIVAERQQEYKEklQGICDLLTQTenrlighQEAFMIGDGTVELKKYQSK-QEELQKDM 1281
Cdd:pfam15921   83 YSHQVKDLQRRLN------ESNELHEKQKFYLR--QSVIDLQTKL-------QEMQMERDAMADIRRRESQsQEDLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1282 QGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKK-------------ELDKVVTTAIK 1348
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrSLGSAISKILR 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1349 EETEKVAAVK--------QLEESKTKIENLLDWLSNVDKDS-ERAGTKHKqvIEQNGTHFQEGDGKSA---------IGE 1410
Cdd:pfam15921  228 ELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRiEQLISEHE--VEITGLTEKASSARSQansiqsqleIIQ 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1411 EDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEE---KEKLQKNMKE 1487
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLAD 385

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1488 LKVHYETALAESEKKMKL----------THSLQEELEKFDADYTEFEHWLQQSEQELE-NLEAGADDINGLMTKLKRQKS 1556
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSS 465

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1557 FSEDVISHKGDLRYITisgnRVLEAAKSCSKRDGGKV-DTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQ 1635
Cdd:pfam15921  466 LTAQLESTKEMLRKVV----EELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD 541

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1636 HYEDASCgllaglqACEATASKHLSEPIAVDPknLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARG------SLL 1709
Cdd:pfam15921  542 HLRNVQT-------ECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelqefKIL 612

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1710 PAKNDIQktLDDIVGRYEDLS----KSVNERNEKLQitltrslSVQDGLDEMLDWMGNVESSLKEqgqvplnstaLQDII 1785
Cdd:pfam15921  613 KDKKDAK--IRELEARVSDLElekvKLVNAGSERLR-------AVKDIKQERDQLLNEVKTSRNE----------LNSLS 673

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1786 SKNIMLEQDIAGRQSSINAMNEKVKKFMEttdpSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEK 1865
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNKLKMQLK----SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1866 LQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHS----LLKEISSHGLPSDKAlvlektnnlSKKF 1941
Cdd:pfam15921  750 IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSqerrLKEKVANMEVALDKA---------SLQF 820

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|..
gi 34577049   1942 KEMEDTI-KEKKEAVT-SCQEQLDafqvlVKSLK--SWIKETTKKVPIVQPS 1989
Cdd:pfam15921  821 AECQDIIqRQEQESVRlKLQHTLD-----VKELQgpGYTSNSSMKPRLLQPA 867
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1660-1741 1.02e-04

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: 44.62  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1660 SEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKNDIQKTLDDIVGRYEDLSKSVNERNEK 1739
Cdd:pfam00435   26 SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERKQK 102


                   ..
gi 34577049   1740 LQ 1741
Cdd:pfam00435  103 LE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 375-469 1.91e-04

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: 43.85  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    375 LHNFVSRATNELIWLNEKEE----EEVAYDWSErntnIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTI 450
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                           90
                   ....*....|....*....
gi 34577049    451 EAYRAAMQTQWSWILQLCQ 469
Cdd:pfam00435   79 QERLEELNERWEQLLELAA 97
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4187-4289 1.95e-04

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: 43.85  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4187 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYfSQKQDVVLIKNLL 4266
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|...
gi 34577049   4267 ISVQSRWEKVVQRLVERGRSLDD 4289
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1751-1958 2.98e-04

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: 45.51  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1751 QDGLDEMLDWMGNVESSLKEQgQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEtTDPSTASSLQAKMKD 1830
Cdd:cd00176    6 LRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERLEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1831 LSARFSEASHKHKETLAKMEELKTKVELFENLSEkLQTFLETKTQALTEVDVPG--KDVTELSQYMQESTSEFLEHKKHL 1908
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEPRL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 34577049 1909 EVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSC 1958
Cdd:cd00176  163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3859-3961 3.66e-04

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: 43.08  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3859 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81

                           90       100
                   ....*....|....*....|...
gi 34577049   3939 LMELKLIWDSLEERIINRQHKLE 3961
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
PTZ00121 PTZ00121
MAEBL; Provisional
 858-1517 6.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   858 AEALVKLYETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALE-----DELQKAKAI--SDEMFKTYKERDLD 930
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkaDELKKAEEKkkADEAKKAEEKKKAD 1305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   931 ------------------FDWHKEKADQLVERWQNVHVQIDNRLRDLEGIGKSLKYYRDTYHP----LDDWIQQVETTQR 988
Cdd:PTZ00121 1306 eakkkaeeakkadeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkKEEAKKKADAAKK 1385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   989 KIQE-NQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSatvKDYELQTMTYRAMVDSQQKSPVKRRRMQSSA 1067
Cdd:PTZ00121 1386 KAEEkKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1068 DLIIQEFMDL-RTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTLKDAEKAGKPPFS 1146
Cdd:PTZ00121 1463 KKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1147 KQKISSEEIStKKEQLSEALQTIQLFLAKHG--DKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSgdvKVEEK 1224
Cdd:PTZ00121 1543 EEKKKADELK-KAEELKKAEEKKKAEEAKKAeeDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK---KAEEA 1618

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1225 IVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQ--SKQEELQKDMQGSAQALAEVVKNTENFLKEN 1302
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1303 GEKLSQEDkalIEQKLNEAKIKCEQL-------NLKAEQSKKELDkvvttaikEETEKVAAVKQLEESKTKIENLldwLS 1375
Cdd:PTZ00121 1699 EEAKKAEE---LKKKEAEEKKKAEELkkaeeenKIKAEEAKKEAE--------EDKKKAEEAKKDEEEKKKIAHL---KK 1764

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1376 NVDKDSERAGTKHKQVIEQNgthFQEGDGKSAIGEEDEVNgnlletDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAV 1455
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIK------DIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049  1456 IIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFD 1517
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD 1897
SPEC smart00150
Spectrin repeats;
3092-3194 6.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 6.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3092 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLkVLSSREDKDMVQSK 3171
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3172 LDFSQVWYIEIQEKSHSRSELLQ 3194
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 868-1032 2.90e-03

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: 42.43  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  868 KLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEdelQKAKAISDEmfktykeRDLDFDWHKEKADQLVERWQN 947
Cdd:cd00176   21 ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN---ELGEQLIEE-------GHPDAEEIQERLEELNQRWEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  948 VHVQIDNRLRDLEGIGKSLKYYRDTYHpLDDWIQqvETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQK 1027
Cdd:cd00176   91 LRELAEERRQRLEEALDLQQFFRDADD-LEQWLE--EKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167


                 ....*
gi 34577049 1028 YAEQY 1032
Cdd:cd00176  168 LAEEL 172
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 627-1368 3.30e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 44.27  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    627 NRIEQQYQNVLTlwHESHINMKSVVSWHYLINEIDRIRASNVASIKTmlpgehqQVLSNLQSRFEDFLEDSQESQVFSGS 706
Cdd:TIGR01612 1029 NDIEQKIEDANK--NIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK-------EILEEAEINITNFNEIKEKLKHYNFD 1099

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    707 DITqleKEVNVckQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIrtplerDDLhESVFRITEQEKL 786
Cdd:TIGR01612 1100 DFG---KEENI--KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI------NDL-EDVADKAISNDD 1167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    787 KKELERLKDDLGTITNKCEEFFSqaaasssvptlrsELNVVLQNMNQVySMSSTYIDKLKTVNLvlkntQAAEALVKLYE 866
Cdd:TIGR01612 1168 PEEIEKKIENIVTKIDKKKNIYD-------------EIKKLLNEIAEI-EKDKTSLEEVKGINL-----SYGKNLGKLFL 1228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    867 TKLCEEeaviadKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEM--FKTYKERDLDFDWHKEKADQLVER 944
Cdd:TIGR01612 1229 EKIDEE------KKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMetFNISHDDDKDHHIISKKHDENISD 1302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    945 WQNvhvqidnrlrdlegigKSLKYYRDTYHPLDdwIQQVETT-QRKIQENQPENSKtLATQLNQQKMLVSEIEMKQSK-- 1021
Cdd:TIGR01612 1303 IRE----------------KSLKIIEDFSEESD--INDIKKElQKNLLDAQKHNSD-INLYLNEIANIYNILKLNKIKki 1363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1022 MDECQKYA---EQYSATVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSAD-----LIIQEFMDLRTRYTALVTLMTQYIK 1093
Cdd:TIGR01612 1364 IDEVKEYTkeiEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDdkdidECIKKIKELKNHILSEESNIDTYFK 1443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1094 ------------FAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNI--SKTLKDAEKAGKPPFSKQKISSEEIstkK 1159
Cdd:TIGR01612 1444 nadennenvlllFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIdkSKGCKDEADKNAKAIEKNKELFEQY---K 1520

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1160 EQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSgDVKVEEKiVAERQQEYKEKLqG 1239
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE-KFRIEDD-AAKNDKSNKAAI-D 1597

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1240 ICDLLTQTENRLIGHQE-AFMIGDGTVELKKYQSKQEELQKDMQGSaqALAEVVKNTeNFLKENGEKLSQEDKALIEQK- 1317
Cdd:TIGR01612 1598 IQLSLENFENKFLKISDiKKKINDCLKETESIEKKISSFSIDSQDT--ELKENGDNL-NSLQEFLESLKDQKKNIEDKKk 1674

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|..
gi 34577049   1318 -LNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEETekVAAVKQLEESKTKIE 1368
Cdd:TIGR01612 1675 eLDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIA--IANKEEIESIKELIE 1724
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2195-2423 5.21e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2195 QELNQLtidrQQKLEESSNNLTQFQT------VEAQLKQwlVEKELmvsvlgplsidpNMLNTQRQQVQILLQEFATRKP 2268
Cdd:COG3206  182 EQLPEL----RKELEEAEAALEEFRQknglvdLSEEAKL--LLQQL------------SELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2269 QYEQLTAAGQGILSRPGEDPSLRGIvKEQLAAVTQKWDSLTGQLSDrcdwidqaivKSTQYQSLLRSLSDKLSDLDNKLS 2348
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQL-RAQLAELEAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQ 312

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 2349 SSLAvsthpdAMNQQLETAQKMKQEIQQEKKQIKvaqalcEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAE 2423
Cdd:COG3206  313 RILA------SLEAELEALQAREASLQAQLAQLE------ARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3535-3630 8.13e-03

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: 39.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3535 EELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLY 3614
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89

                           90
                   ....*....|....*.
gi 34577049   3615 SQIKEDVKKRAVALDE 3630
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3092-3195 9.88e-03

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: 38.84  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3092 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSK 3171
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|....
gi 34577049   3172 LDFSQVWyIEIQEKSHSRSELLQQ 3195
Cdd:pfam00435   83 EELNERW-EQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 4864-4942 1.25e-37

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 137.19  E-value: 1.25e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049    4864 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRAKG 4942
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3967-4182 9.91e-36

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: 137.19  E-value: 9.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3967 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 4046
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4047 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 4126
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 4127 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 4182
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 4866-4940 9.97e-35

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 128.87  E-value: 9.97e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34577049   4866 IEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRA 4940
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
 651-728 6.01e-34

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


Pssm-ID: 465730  Cd Length: 78  Bit Score: 126.95  E-value: 6.01e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049    651 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 728
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4406-4618 2.29e-31

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: 124.48  E-value: 2.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4406 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4486 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 4565
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4566 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 4618
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4293-4509 1.15e-26

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: 111.00  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4293 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 4372
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4373 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 4452
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 4453 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 4509
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4184-4401 1.09e-25

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: 108.30  E-value: 1.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4184 LAMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIK 4263
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4264 NLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWsKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLG 4343
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 4344 AKHSVYDTTNRTGRSLKEKTSLADDNlKLDDMLSELRDKWDTICGKSVERQNKLEEAL 4401
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3859-4073 5.68e-23

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: 100.21  E-value: 5.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3859 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3939 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 4018
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 4019 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 4073
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3747-3964 7.84e-21

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: 94.05  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3747 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 3826
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3827 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 3906
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3907 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 3964
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
 550-616 1.21e-20

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.21e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049    550 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 616
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4075-4291 1.49e-20

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: 93.28  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4075 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 4154
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4155 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 4234
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 4235 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 4291
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 375-557 4.99e-19

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: 89.04  E-value: 4.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  375 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 454
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  455 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 534
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158

                        170       180
                 ....*....|....*....|...
gi 34577049  535 KSTIANLMGKAKTIIQLKPRNSD 557
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAD 181
SPEC smart00150
Spectrin repeats;
3969-4070 3.12e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.07  E-value: 3.12e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3969 QFQHALDELLAWLTHTEGLLSeQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 4048
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    4049 EVLNQRWQNVLEKTEQRKQQLD 4070
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2870-3085 5.75e-17

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: 82.88  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2870 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 2949
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2950 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKVvKAQIQEQKLLQRL 3029
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049 3030 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 3085
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3529-3745 7.51e-17

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: 82.49  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3529 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 3608
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3609 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 3688
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3689 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 3745
Cdd:cd00176  161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 282-477 1.77e-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: 81.72  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  282 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISE---IQMTAPLKLTYAEKLHRLESQY 358
Cdd:cd00176    9 ADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGeqlIEEGHPDAEEIQERLEELNQRW 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  359 AKLLNTSRNQERHLDT---LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEI 435
Cdd:cd00176   89 EELRELAEERRQRLEEaldLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNEL 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 34577049  436 AEQLLLENHP-ARLTIEAYRAAMQTQWSWILQLCQCVEQHIKE 477
Cdd:cd00176  169 AEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2984-3197 1.82e-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: 81.34  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2984 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 3063
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3064 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHN 3143
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34577049 3144 KHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHSRSELLQQAL 3197
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3419-3632 2.72e-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: 80.95  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3419 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 3498
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3499 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 3578
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 3579 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 3632
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2102-2323 8.79e-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: 79.41  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2102 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 2181
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2182 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 2261
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2262 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 2323
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3637-3854 1.14e-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: 79.03  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3637 QFHDKIDQILESLERIVERLRQPpSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGtdkdiSAKAV 3716
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3717 QDKLDQMVFIWENIHTLVEEREAKLLDVMELAEKFWcDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEI 3796
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3797 DGLQEELDIVINLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEEAM 3854
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 4511-4758 4.07e-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: 77.49  E-value: 4.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4511 QAEEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTIK 4590
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4591 HWITIIRARFEEVLAWAKQHQQRLASALAgliaKQELLEALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEE 4670
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALD----LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4671 MTRKQPDVDKVTKTykrraadpsslqshipvldkgragrkrfpASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALER 4750
Cdd:cd00176  155 LEAHEPRLKSLNEL-----------------------------AEELLEEGHPDADEEIEEKLEELNERWEELLELAEER 205


                 ....*...
gi 34577049 4751 RRKLNDAL 4758
Cdd:cd00176  206 QKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2328-2542 6.37e-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: 77.10  E-value: 6.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2328 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 2405
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2406 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 2485
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 2486 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 2542
Cdd:cd00176  157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3091-3306 1.79e-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: 72.86  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3091 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLkVLSSREDKDMVQS 3170
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3171 KLDFSQVWYIEIQEKSHSRSELLQQALCNAKIFgEDEVELMNWLNEvhdKLSKLSVQDY--STEGLWKQQSELRVLQEDI 3248
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEE---KEAALASEDLgkDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 3249 LLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 3306
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3969-4069 2.07e-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: 69.27  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3969 QFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 4048
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82

                           90       100
                   ....*....|....*....|.
gi 34577049   4049 EVLNQRWQNVLEKTEQRKQQL 4069
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1512-1741 2.72e-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: 72.09  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1512 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 1591
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1592 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 1671
Cdd:cd00176   76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1672 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 1741
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
4406-4506 4.44e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.13  E-value: 4.44e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4406 QFTDALQALIDWLYRVEPQLAeDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049    4486 ELSTRWETVCALSISKQTRLE 4506
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2437-2623 1.19e-12

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: 70.55  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2437 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLlKTQGSEKAALQLQ 2516
Cdd:cd00176    3 QQFLRDADELEAWLS-EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2517 LNTIKTNWDTFNKQVKERENKLKESLEKALKYkEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHF 2596
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180
                 ....*....|....*....|....*..
gi 34577049 2597 GMVELLNNTANSLLSVCEIDKEVVTDE 2623
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEE 186
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3308-3523 1.50e-12

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: 70.17  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3308 LARRLHSTHEELCTWLDKVEVELLSyeTQVLKGEEASQAQMRP-KELKKEAKNNKALLDSLNEVSSALLELVPWRAREgL 3386
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKhEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3387 EKMVAEDNERYRLVSDTITQKVEEIDAAiLRSQQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEI 3466
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 3467 LRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERA 3523
Cdd:cd00176  156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
4079-4179 6.81e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.96  E-value: 6.81e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4079 FHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNIDQDIN 4158
Cdd:smart00150    3 FLRDADELEAWLEEKEQ-LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049    4159 NLKEKWESVETKLNERKTKLE 4179
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4296-4398 1.17e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 1.17e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4296 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSlaDDNLKLDDM 4375
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    4376 LSELRDKWDTICGKSVERQNKLE 4398
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4789-4851 1.48e-10

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: 59.87  E-value: 1.48e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALH 4851
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4789-4852 1.93e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 1.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEmsAVADIFDRDGDGYIDYYEFVAALHP 4852
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD--ELFARLDTDGDGKISFEEFVAAVRD 131
SPEC smart00150
Spectrin repeats;
376-476 4.46e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 4.46e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049     376 HNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRA 455
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049     456 AMQTQWSWILQLCQCVEQHIK 476
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1185-1983 5.57e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 5.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1185 RNELEKQVKTLQ------ESYNLLfSESLKQLQESQTSGDVKVEEKIVAERQQEYKEkLQGICDLLTQTENRLIGHQEAF 1258
Cdd:TIGR02168  195 LNELERQLKSLErqaekaERYKEL-KAELRELELALLVLRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1259 MIGDGTVElKKYQSKQEELQ------KDMQGSAQALAEVVKNTENFLKENGEKL---------SQEDKALIEQKLNEAKI 1323
Cdd:TIGR02168  273 RLEVSELE-EEIEELQKELYalaneiSRLEQQKQILRERLANLERQLEELEAQLeeleskldeLAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1324 KCEQLNLK---AEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQ 1400
Cdd:TIGR02168  352 ELESLEAEleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1401 EGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEK 1480
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQ------EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEG 503

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1481 LQKNMKELKvhyetalaESEKKMKLTHSLQEELEKFDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSF 1557
Cdd:TIGR02168  504 FSEGVKALL--------KNQSGLSGILGVLSELISVDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTF 575

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1558 SE-DVISH---KGDLRYITISGNRVLEAAKSCSKRD-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkc 1620
Cdd:TIGR02168  576 LPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG-- 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1621 nvlgnnlkDLVdkyqhyedASCGLLAGlqACEATASKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEV 1700
Cdd:TIGR02168  653 --------DLV--------RPGGVITG--GSAKTNSSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEE 709

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1701 LLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN---ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLN 1777
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLE----------------EA 773

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1778 STALQDIISKNIMLEQDIAGRQSSINAMNEKVkkfmettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVE 1857
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREAL------------DELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1858 LFENLSEKLQtfletktqaltevdvpgKDVTELSQYMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNL 1937
Cdd:TIGR02168  842 DLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEEL 899

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*.
gi 34577049   1938 SKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKV 1983
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4749-4850 1.60e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4749 ERRRKLNDALDRLE-------ELREFANFDFDIWRkkymrwmnhkksrvmDFFRRIDKDQDGKITRQEFIDGILSSKFPT 4821
Cdd:COG5126    2 LQRRKLDRRFDLLDadgdgvlERDDFEALFRRLWA---------------TLFSEADTDGDGRISREEFVAGMESLFEAT 66

                         90       100
                 ....*....|....*....|....*....
gi 34577049 4822 SRLEMSAVADIFDRDGDGYIDYYEFVAAL 4850
Cdd:COG5126   67 VEPFARAAFDLLDTDGDGKISADEFRRLL 95
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2223-2432 2.26e-09

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: 60.92  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2223 AQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSrpgEDPSLRGIVKEQLAAVT 2302
Cdd:cd00176   10 DELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDAEEIQERLEELN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2303 QKWDSLTGQLSDRCDWIDQAIvkstQYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQ 2380
Cdd:cd00176   86 QRWEELRELAEERRQRLEEAL----DLQQFFRDADDLEQWLEEKEAalASEDLGKDLESVEELLKKHKELEEELEAHEPR 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2381 IKVAQALCEDLSALvKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSA 2432
Cdd:cd00176  162 LKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 3209-3415 3.14e-09

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: 60.54  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3209 ELMNWLNEVHDKLSKLSVQDySTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQTtGDEVLIIQDKLEAIKARY 3288
Cdd:cd00176   11 ELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELNQRW 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 3289 KDITKLSTDVAKTLEQALQLARRLHStHEELCTWLDKVEVELLSYEtqVLKGEEASQAQM-RPKELKKEAKNNKALLDSL 3367
Cdd:cd00176   89 EELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELLkKHKELEEELEAHEPRLKSL 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 34577049 3368 NEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAI 3415
Cdd:cd00176  166 NELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4513-4614 4.44e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.95  E-value: 4.44e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4513 EEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTIKHW 4592
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDA-EEIEER 78

                            90       100
                    ....*....|....*....|..
gi 34577049    4593 ITIIRARFEEVLAWAKQHQQRL 4614
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
2984-3085 1.13e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.80  E-value: 1.13e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2984 RFQDALESLLSWMVDTEELVAnQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 3063
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    3064 SLLDSRWEALLNKAETRNRQLE 3085
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2763-2979 1.52e-08

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: 58.23  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2763 HFQNTIREMFSQFAEFDDELDSMAPvGRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLatEETSPDLVGIKRD 2842
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI--EEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2843 LEALSKQCNKLLDRAQAREEQVEGTIKRLEeFYSKLKEFSILLQKAEEHEESQgPVGMETETINQQLNMFKVFQkEEIEP 2922
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELE-EELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049 2923 LQGKQQDVNWLGQGLIQSAAkSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEAL 2979
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGH-PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4079-4180 2.29e-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: 55.02  E-value: 2.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4079 FHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNIDQDIN 4158
Cdd:pfam00435    6 FFRDADDLESWIEEKEA-LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 34577049   4159 NLKEKWESVETKLNERKTKLEE 4180
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2104-2209 3.53e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.26  E-value: 3.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2104 QKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAPRW 2183
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEI 75

                            90       100
                    ....*....|....*....|....*.
gi 34577049    2184 KQMLTEIDSKWQELNQLTIDRQQKLE 2209
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
EF-hand_7 pfam13499
EF-hand domain pair;
4787-4850 6.28e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.26  E-value: 6.28e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049   4787 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 4850
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPEC smart00150
Spectrin repeats;
2437-2539 7.33e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 7.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2437 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 2516
Cdd:smart00150    1 QQFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQ-LIEEGHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    2517 LNTIKTNWDTFNKQVKERENKLK 2539
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3749-3851 8.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 8.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3749 EKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKS 3828
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3829 IDELNSAWDSLNKAWKDRIDKLE 3851
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2102-2210 1.57e-07

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: 52.71  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2102 KLQKAQEESSAMMQWLQKMNKTATkwqQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 2181
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASE 76

                           90       100
                   ....*....|....*....|....*....
gi 34577049   2182 RWKQMLTEIDSKWQELNQLTIDRQQKLEE 2210
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4187-4288 2.12e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 2.12e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    4187 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIKNLL 4266
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 34577049    4267 ISVQSRWEKVVQRLVERGRSLD 4288
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3859-3961 2.78e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 2.78e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3859 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--IEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3939 LMELKLIWDSLEERIINRQHKLE 3961
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 4792-4851 2.99e-07

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 50.30  E-value: 2.99e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4792 DFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLemSAVADIFDRDGDGYIDYYEFVAALH 4851
Cdd:cd00052    3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL--AQIWDLADTDKDGKLDKEEFAIAMH 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2333-3134 3.74e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2333 LRSLSDKLSDLDNKLSSSLAVSTHpDAMNQQLETAQKMKQEIQQEKKQIKVAQalcEDLSALVKEEYLKAELSRQLEGIL 2412
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2413 KSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKS-HPISAKLDVLeslikdhkdfsktltaqshmy 2491
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElAELEEKLEEL--------------------- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2492 eKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKF 2571
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2572 CLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANsllsvcEIDKEVvtDENKSLIQKVDMVTEQLHSKKFCLENMTQK 2651
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREEL--EEAEQALDAAERELAQLQARLDSLERLQEN 500

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2652 FKEFQEVSKEskrQLQCAKEQLDIHDSLGSQaysnkyltmLQTQQKSLQALkhQVDLAKRLaQDLVVEASDSkgtsdVLL 2731
Cdd:TIGR02168  501 LEGFSEGVKA---LLKNQSGLSGILGVLSEL---------ISVDEGYEAAI--EAALGGRL-QAVVVENLNA-----AKK 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2732 QVETIAQEHSTlsqqvdeKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAPVGRDA-----------ETLQk 2797
Cdd:TIGR02168  561 AIAFLKQNELG-------RVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLD- 632

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2798 qkeTIKAFLKKLEALM--------------ASNDNANKTCKMMLAT----EETSPDLVGIKRDLEALSKQCNKLLDRAQA 2859
Cdd:TIGR02168  633 ---NALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEE 709

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2860 REEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQ 2939
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2940 SAAK-STSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKA 3018
Cdd:TIGR02168  790 QIEQlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3019 QIQEQklLQRLLDDRKSTVEVIKREGEKIATTAEPADKVkiLKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETL 3098
Cdd:TIGR02168  870 ELESE--LEALLNERASLEEALALLRSELEELSEELREL--ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945

                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 34577049   3099 epLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHKA 3134
Cdd:TIGR02168  946 --SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3773-3852 4.96e-07

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: 51.17  E-value: 4.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3773 EDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEE 3852
Cdd:pfam00435   27 EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4296-4399 5.63e-07

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: 50.78  E-value: 5.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4296 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKLDDM 4375
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 34577049   4376 LSELRDKWDTICGKSVERQNKLEE 4399
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2071-2211 5.73e-07

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: 53.60  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2071 IKKDMTDISHGYEDLGLLLKDKIAELNTKLsKLQKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFE 2150
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL---ASEDLGKDLESVEELLKKHKELE 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34577049 2151 AELKQNVNKVQELKDKLTELLEENPDTPEAPRwKQMLTEIDSKWQELNQLTIDRQQKLEES 2211
Cdd:cd00176  153 EELEAHEPRLKSLNELAEELLEEGHPDADEEI-EEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4406-4507 6.03e-07

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: 50.78  E-value: 6.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4406 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 4485
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 34577049   4486 ELSTRWETVCALSISKQTRLEA 4507
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
3529-3629 8.45e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 8.45e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3529 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 3608
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 34577049    3609 AADTLYSQIKEDVKKRAVALD 3629
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 1262-2245 8.82e-07

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 55.83  E-value: 8.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1262 DGTVELKKYqsKQEELQKDMQgsaqALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKC---EQL---NLKAEQS 1335
Cdd:TIGR01612  736 DIIVEIKKH--IHGEINKDLN----KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhynDQInidNIKDEDA 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1336 KKELDKvvttaiKEETEKVAAVKQLEESKT--KIENLLD-WLSNVDKDSERAgTKHKQVIEQNGTHFQEGDGKSAIGEED 1412
Cdd:TIGR01612  810 KQNYDK------SKEYIKTISIKEDEIFKIinEMKFMKDdFLNKVDKFINFE-NNCKEKIDSEHEQFAELTNKIKAEISD 882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1413 EvNGNLLETDVDGQ---VGTTQENLNQQYQKVKAQhEKIISQHQAVIIATQSAQVLLEKQGQYlspeeKEKLQKNMKELK 1489
Cdd:TIGR01612  883 D-KLNDYEKKFNDSkslINEINKSIEEEYQNINTL-KKVDEYIKICENTKESIEKFHNKQNIL-----KEILNKNIDTIK 955

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1490 vhyETALAESEKKMKLTHSLQEELEKFDADYTEfehwLQQSEQELENLEAgADDINGLMTKLKRQKsfsEDVISHKGDLR 1569
Cdd:TIGR01612  956 ---ESNLIEKSYKDKFDNTLIDKINELDKAFKD----ASLNDYEAKNNEL-IKYFNDLKANLGKNK---ENMLYHQFDEK 1024

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1570 YITISG--NRVLEAAKSCSKRDGGkVDTSATH--REVQRKLDHATDRF-RSLYSKCNVLGNNLKDLVDKYQHYEDASCGL 1644
Cdd:TIGR01612 1025 EKATNDieQKIEDANKNIPNIEIA-IHTSIYNiiDEIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFDDFGK 1103

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1645 LAGLqaceatasKHLSEpiavdpknLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLpakNDIQKTLDDIVg 1724
Cdd:TIGR01612 1104 EENI--------KYADE--------INKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI---NDLEDVADKAI- 1163

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1725 rYEDLSKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESslkeqgqvplNSTALQDIisKNIMLEQDIAGRQSSINA 1804
Cdd:TIGR01612 1164 -SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEK----------DKTSLEEV--KGINLSYGKNLGKLFLEK 1230

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1805 MNEKVKKfmettDPSTASSLQAKMKDLSaRFSEASHKHKETLAKMEELKTKVELFENLSEKLQTF-------------LE 1871
Cdd:TIGR01612 1231 IDEEKKK-----SEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiiskkhdenisdIR 1304

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1872 TKTQALTEVDVPGKDVTELSQYMQEStseFLEHKKHLEVLHSLLKEISShglpSDKALVLEKTNNLSKKFKEMEDTIKEK 1951
Cdd:TIGR01612 1305 EKSLKIIEDFSEESDINDIKKELQKN---LLDAQKHNSDINLYLNEIAN----IYNILKLNKIKKIIDEVKEYTKEIEEN 1377

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1952 KEAVTScqeQLDAFQVLVKSLKSWIKETTKKVPIvQPSFGAEDLGKSLEDTKK-----LQEKWSLKTP-EIQKVNNSGIS 2025
Cdd:TIGR01612 1378 NKNIKD---ELDKSEKLIKKIKDDINLEECKSKI-ESTLDDKDIDECIKKIKElknhiLSEESNIDTYfKNADENNENVL 1453

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2026 LcnLISAVttpakAIAAVKSGGAVLNGEGTATNTEEFWANKgltsiKKDMTDISHGYEDlglllkdkiaelntKLSKLQK 2105
Cdd:TIGR01612 1454 L--LFKNI-----EMADNKSQHILKIKKDNATNDHDFNINE-----LKEHIDKSKGCKD--------------EADKNAK 1507

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2106 AQEESSAMM-QWLQKMNKTATKWQQTpaptdteAVKTQVEQNKSfeaELKQNVNKVQELKDKLTELLEENPDTPEAPRWK 2184
Cdd:TIGR01612 1508 AIEKNKELFeQYKKDVTELLNKYSAL-------AIKNKFAKTKK---DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE 1577

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049   2185 QMLTEID-SKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPLSID 2245
Cdd:TIGR01612 1578 KFRIEDDaAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSID 1639
SPEC smart00150
Spectrin repeats;
3419-3521 9.59e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 9.59e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3419 QQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTAcSEEEKQSMKKK 3498
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3499 LDKVLKNYDTICQINSERYLQLE 3521
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2544-2755 1.13e-06

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: 52.83  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2544 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 2623
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2624 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 2703
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34577049 2704 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 2755
Cdd:cd00176  160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1264-1978 1.15e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1264 TVELKKYQSKQEELQKDMQG-SAQALAEVVKNTENFLKENGEKLSQEDKAL--IEQKLNEAKIKCEQLNLKAEQSKKELD 1340
Cdd:TIGR02168  212 AERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELqeLEEKLEELRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1341 KVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDE---VNGN 1417
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaelEELE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1418 LLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAViiatQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALA 1497
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1498 ESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKL-------------KRQKSFSEDVISH 1564
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvkallknQSGLSGILGVLSE 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1565 K----------------GDLRYITISG-NRVLEAAKSCSKRDGGKVDTSATHREVQRKLDhaTDRFRSLYSKCNVLGnNL 1627
Cdd:TIGR02168  528 LisvdegyeaaieaalgGRLQAVVVENlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ--GNDREILKNIEGFLG-VA 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1628 KDLVDKYQHYEDASCGLLAGL-------QACEATASKHLSEPI----------------AVDPKN---LQRQLE------ 1675
Cdd:TIGR02168  605 KDLVKFDPKLRKALSYLLGGVlvvddldNALELAKKLRPGYRIvtldgdlvrpggvitgGSAKTNssiLERRREieelee 684

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1676 ETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN---ERNEKLQITLTRSLSVQD 1752
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIE 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1753 GLDEMLDwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFME---------TTDPSTASS 1823
Cdd:TIGR02168  765 ELEERLE----------------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeaANLRERLES 828

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1824 LQAKMKDLSARFSEASHKHKETLAKME----ELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTS 1899
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049   1900 EFLEHKKHLEVLHSLLKEISSHgLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFqvlVKSLKSWIKE 1978
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELR-LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR---LKRLENKIKE 983
SPEC smart00150
Spectrin repeats;
282-373 1.65e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.64  E-value: 1.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049     282 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 358
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86

                            90
                    ....*....|....*
gi 34577049     359 AKLLNTSRNQERHLD 373
Cdd:smart00150   87 EELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2437-2540 2.67e-06

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: 48.85  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2437 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 2516
Cdd:pfam00435    4 QQFFRDADDLESWIE-EKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEK-LIDEGHYASEEIQER 81

                           90       100
                   ....*....|....*....|....
gi 34577049   2517 LNTIKTNWDTFNKQVKERENKLKE 2540
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1635-1741 4.88e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 4.88e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    1635 QHYEDASCGLLAGLQACEATASkhlSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKND 1714
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA---SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH---PDAEE 74

                            90       100
                    ....*....|....*....|....*..
gi 34577049    1715 IQKTLDDIVGRYEDLSKSVNERNEKLQ 1741
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3416-3522 1.02e-05

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: 47.31  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3416 LRSQQFDQAADAELSWITETEKKLMSlGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQsM 3495
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-I 78

                           90       100
                   ....*....|....*....|....*..
gi 34577049   3496 KKKLDKVLKNYDTICQINSERYLQLER 3522
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4510-4614 2.20e-05

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: 46.54  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4510 RQAEEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTI 4589
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEI 78

                           90       100
                   ....*....|....*....|....*
gi 34577049   4590 KHWITIIRARFEEVLAWAKQHQQRL 4614
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2362-3097 2.49e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2362 QQLETAQKMKqEIQQEKKQIKVAqalcedLSALVKEEYLKaelsrQLEGILKSFKDVEQKAENHVQHLQSACASSHQFqq 2441
Cdd:TIGR02168  207 RQAEKAERYK-ELKAELRELELA------LLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEEL-- 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2442 msRDFQAWLDTKKEEQNKS-HPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQgSEKAALQLQLNTI 2520
Cdd:TIGR02168  273 --RLEVSELEEEIEELQKElYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-EELAELEEKLEEL 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2521 KTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKfcldpaegensiAKLKSLQKEMDQHFGMVE 2600
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN------------NEIERLEARLERLEDRRE 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2601 LLNNTANSLLsvceidKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLg 2680
Cdd:TIGR02168  418 RLQQEIEELL------KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR- 490

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2681 sqaysnkyLTMLQTQQKSLQ--------ALKHQVDLAK---RLAQDLVVEASDSKGTSDVL---LQ------VETIAQEH 2740
Cdd:TIGR02168  491 --------LDSLERLQENLEgfsegvkaLLKNQSGLSGilgVLSELISVDEGYEAAIEAALggrLQavvvenLNAAKKAI 562

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2741 STLSQQVDEKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAP------------------------------ 2787
Cdd:TIGR02168  563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPklrkalsyllggvlvvddldnalelakklr 642

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2788 ------------------------------VGRDAE------TLQKQKETIKAFLKKLEALMASNDNA-NKTCKMMLATE 2830
Cdd:TIGR02168  643 pgyrivtldgdlvrpggvitggsaktnssiLERRREieeleeKIEELEEKIAELEKALAELRKELEELeEELEQLRKELE 722

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2831 ETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQgpvgmeTETINQQLN 2910
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------EAQIEQLKE 796

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2911 MFKVfQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQG-LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDAL 2989
Cdd:TIGR02168  797 ELKA-LREALDELRAELTLLNEEAANLRERLESLERRIAaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2990 ESLLSWMVDTEELVA------------------------------NQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEV 3039
Cdd:TIGR02168  876 EALLNERASLEEALAllrseleelseelreleskrselrreleelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3040 IKREGEKIATTAEPA-DKVKILKQ---------------LSLLDSRWEAL------LNKA-------------ETRNRQL 3084
Cdd:TIGR02168  956 AEALENKIEDDEEEArRRLKRLENkikelgpvnlaaieeYEELKERYDFLtaqkedLTEAketleeaieeidrEARERFK 1035

                          890
                   ....*....|...
gi 34577049   3085 EGISVVAQQFHET 3097
Cdd:TIGR02168 1036 DTFDQVNENFQRV 1048
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 710-1517 3.46e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.74  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    710 QLEKEVNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKE 789
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    790 LERLKDDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQ----VYSMSSTYIDKLKTVNLVLKNTQAAEalvkLY 865
Cdd:pfam02463  281 KKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKkaekELKKEKEEIEELEKELKELEIKREAE----EE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    866 ETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVE-- 943
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEee 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    944 ---RWQNVHVQIDNRLRDLEGIGKSLKYYRDTyhPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQS 1020
Cdd:pfam02463  437 esiELKQGKLTEEKEELEKQELKLLKDELELK--KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1021 KM--------DECQKYAEQYSATVKDYELQTMTYRAMVDSQQKSPVKRRR------------MQSSADLIIQEFMDLRTR 1080
Cdd:pfam02463  515 LIkdgvggriISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQklvraltelplgARKLRLLIPKLKLPLKSI 594

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1081 YTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQ-KWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKK 1159
Cdd:pfam02463  595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1160 EQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLF----SESLKQLQESQTSGDVKVEEKIVAERQQEYkE 1235
Cdd:pfam02463  675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEaeelLADRVQEAQDKINEELKLLKQKIDEEEEEE-E 753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1236 KLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIE 1315
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1316 QKLNEAKIKCEQLNLKAE-QSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENlldwlsnvdKDSERAGTKHKQVIEQ 1394
Cdd:pfam02463  834 ELEELALELKEEQKLEKLaEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL---------ESKEEKEKEEKKELEE 904

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1395 NGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQvgttQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQgqyLS 1474
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEE----PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV---NL 977

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 34577049   1475 PEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFD 1517
Cdd:pfam02463  978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2984-3085 4.19e-05

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: 45.77  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2984 RFQDALESLLSWMVDTEELVANQKPPSaEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 3063
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|..
gi 34577049   3064 SLLDSRWEALLNKAETRNRQLE 3085
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 851-1487 4.51e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    851 VLKNTQAAEA-LVKLYETKLCEEEAVIAD-KNNIENLISTLKQWRSEVDEKRQVFH-ALEDELQKAKAISDEMFK----- 922
Cdd:pfam05483  159 LLKETCARSAeKTKKYEYEREETRQVYMDlNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKeindk 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    923 -----------TYKE---RDLDF--DWHKEKADQLVERwqnvhvqidNRLRDlegigKSLKYYRDTYHPLDDWIQQVETT 986
Cdd:pfam05483  239 ekqvsllliqiTEKEnkmKDLTFllEESRDKANQLEEK---------TKLQD-----ENLKELIEKKDHLTKELEDIKMS 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    987 QRKIQENQpensKTLATQLN-QQKMLVSEIEMKQSKMDECQKYAEQYSATVKDYELQTMTYRAMVDSQQKspvkrrRMQS 1065
Cdd:pfam05483  305 LQRSMSTQ----KALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQ------RLEK 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1066 SADLIIQEFMDLRTRYTAL--VTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTLKDAEKagkp 1143
Cdd:pfam05483  375 NEDQLKIITMELQKKSSELeeMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK---- 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1144 pfskqkisseEISTKKEQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSGDVKVEE 1223
Cdd:pfam05483  451 ----------EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1224 KIVAERQQEYK--EKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQE---------ELQKDMQGSAQALAEVV 1292
Cdd:pfam05483  521 DIINCKKQEERmlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENarsieyevlKKEKQMKILENKCNNLK 600

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1293 KNTENFLKeNGEKLSQEDKALIEQ------KLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEetekvaavkqLEESKTK 1366
Cdd:pfam05483  601 KQIENKNK-NIEELHQENKALKKKgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE----------IEDKKIS 669

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1367 IENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEgdgKSAIGEEDEVNGNLLETDVDGQVGTTQeNLNQQYQKVKAQHE 1446
Cdd:pfam05483  670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE---MVALMEKHKHQYDKIIEERDSELGLYK-NKEQEQSSAKAALE 745

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 34577049   1447 KIISQHQAVIIATQSaQVLLEKqgqylspEEKEKLQKNMKE 1487
Cdd:pfam05483  746 IELSNIKAELLSLKK-QLEIEK-------EEKEKLKMEAKE 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2089-2910 6.85e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2089 LKDKIAELNTKLSKLQKaQEESSAMMQWLQKMNKTATKWQQTpapTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLT 2168
Cdd:TIGR02168  191 LEDILNELERQLKSLER-QAEKAERYKELKAELRELELALLV---LRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2169 ELLEENPDtpEAPRWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKElmvsvlgplsidpnm 2248
Cdd:TIGR02168  267 EKLEELRL--EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE--------------- 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2249 lntqrQQVQILLQEFATRKPQYEQLtaagqgilsrpgedpslrgivKEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQ 2328
Cdd:TIGR02168  330 -----SKLDELAEELAELEEKLEEL---------------------KEELESLEAELEELEAELEELESRLEELEEQLET 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2329 YQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAELSRQL 2408
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2409 EGILKSFKDVEQK---AENHVQHLQSACASshqFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLt 2485
Cdd:TIGR02168  464 EELREELEEAEQAldaAERELAQLQARLDS---LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI- 539

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2486 aqshmyEKTIAEG-ENLLLKTQGSEKAALQLQLNTIKTNWdTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQN 2564
Cdd:TIGR02168  540 ------EAALGGRlQAVVVENLNAAKKAIAFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2565 NLEE-IKFCLDPAEGENSIAKLKSLQKEMDQHFGMV----ELLN----------NTANSLLSV------CEIDKEVVTDE 2623
Cdd:TIGR02168  613 KLRKaLSYLLGGVLVVDDLDNALELAKKLRPGYRIVtldgDLVRpggvitggsaKTNSSILERrreieeLEEKIEELEEK 692

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2624 NKSLIQKVDMVTEQlhskkfcLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHdslgsQAYSNKYLTMLQTQQKSLQALK 2703
Cdd:TIGR02168  693 IAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARL-----EAEVEQLEERIAQLSKELTELE 760

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2704 HQvdlAKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLqgighfQNTIREMFSQFAEFDDELD 2783
Cdd:TIGR02168  761 AE---IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL------TLLNEEAANLRERLESLER 831

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2784 SMAPVGRDAETLQKQKETIKAFLKKLEALMASndnanktckmmlatEETSPDlvGIKRDLEALSKQCNKL---LDRAQAR 2860
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIE--ELESELEALLNERASLeeaLALLRSE 895

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|.
gi 34577049   2861 EEQVEGTIKRLEEFYSKLKEFSILLQ-KAEEHEESQGPVGMETETINQQLN 2910
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELReKLAQLELRLEGLEVRIDNLQERLS 946
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1203-1989 8.09e-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: 49.35  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1203 FSESLKQLQESQTsgdvkvEEKIVAERQQEYKEklQGICDLLTQTenrlighQEAFMIGDGTVELKKYQSK-QEELQKDM 1281
Cdd:pfam15921   83 YSHQVKDLQRRLN------ESNELHEKQKFYLR--QSVIDLQTKL-------QEMQMERDAMADIRRRESQsQEDLRNQL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1282 QGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKK-------------ELDKVVTTAIK 1348
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrSLGSAISKILR 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1349 EETEKVAAVK--------QLEESKTKIENLLDWLSNVDKDS-ERAGTKHKqvIEQNGTHFQEGDGKSA---------IGE 1410
Cdd:pfam15921  228 ELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRiEQLISEHE--VEITGLTEKASSARSQansiqsqleIIQ 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1411 EDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEE---KEKLQKNMKE 1487
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLAD 385

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1488 LKVHYETALAESEKKMKL----------THSLQEELEKFDADYTEFEHWLQQSEQELE-NLEAGADDINGLMTKLKRQKS 1556
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSS 465

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1557 FSEDVISHKGDLRYITisgnRVLEAAKSCSKRDGGKV-DTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQ 1635
Cdd:pfam15921  466 LTAQLESTKEMLRKVV----EELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD 541

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1636 HYEDASCgllaglqACEATASKHLSEPIAVDPknLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARG------SLL 1709
Cdd:pfam15921  542 HLRNVQT-------ECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelqefKIL 612

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1710 PAKNDIQktLDDIVGRYEDLS----KSVNERNEKLQitltrslSVQDGLDEMLDWMGNVESSLKEqgqvplnstaLQDII 1785
Cdd:pfam15921  613 KDKKDAK--IRELEARVSDLElekvKLVNAGSERLR-------AVKDIKQERDQLLNEVKTSRNE----------LNSLS 673

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1786 SKNIMLEQDIAGRQSSINAMNEKVKKFMEttdpSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEK 1865
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNKLKMQLK----SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1866 LQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHS----LLKEISSHGLPSDKAlvlektnnlSKKF 1941
Cdd:pfam15921  750 IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSqerrLKEKVANMEVALDKA---------SLQF 820

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|..
gi 34577049   1942 KEMEDTI-KEKKEAVT-SCQEQLDafqvlVKSLK--SWIKETTKKVPIVQPS 1989
Cdd:pfam15921  821 AECQDIIqRQEQESVRlKLQHTLD-----VKELQgpGYTSNSSMKPRLLQPA 867
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1660-1741 1.02e-04

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: 44.62  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1660 SEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKNDIQKTLDDIVGRYEDLSKSVNERNEK 1739
Cdd:pfam00435   26 SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERKQK 102


                   ..
gi 34577049   1740 LQ 1741
Cdd:pfam00435  103 LE 104
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 2082-2657 1.24e-04

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: 48.58  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2082 YEDLGLLLKDKIAELNTKLS-----------KLQKAQEESSAMMQWLQKMNK--------------TATKWQQTPAPTDT 2136
Cdd:pfam15921  215 FRSLGSAISKILRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQdrieqliseheveiTGLTEKASSARSQA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2137 EAVKTQVE--------QNKSFEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEidskwQELNQLTIDRQQKL 2208
Cdd:pfam15921  295 NSIQSQLEiiqeqarnQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN-----SELTEARTERDQFS 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2209 EESSNNLTQFQTVEAQLKQwlVEKELMVSVLGPLSI-DPNMLNTQrqQVQILLQEFATRKPQYEQLTAAGQGILSRpged 2287
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHK--REKELSLEKEQNKRLwDRDTGNSI--TIDHLRRELDDRNMEVQRLEALLKAMKSE---- 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2288 psLRGIVKEQLAAVT------QKWDSLTGQLSDRCDW----IDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHP 2357
Cdd:pfam15921  442 --CQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2358 DAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAELSRQlegilksfkDVEQKAENHVQHLQSACASSH 2437
Cdd:pfam15921  520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQ---------QIENMTQLVGQHGRTAGAMQV 590

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2438 QFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHK-DFSKTLTAQSHMYE--KTIAEGENLLL---KTQGSEKA 2511
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGSERLRavKDIKQERDQLLnevKTSRNELN 670

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2512 ALQLQLNTIKTNWDTFNKQVKERENKLKESLEKAlkykeqvetlwpwidkcQNNLEEIKFCLDPAEGEN--SIAKLKSLQ 2589
Cdd:pfam15921  671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA-----------------QSELEQTRNTLKSMEGSDghAMKVAMGMQ 733

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34577049   2590 KEMDQHFGMVELLNNTANSL---LSVCEIDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQE 2657
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2621-3511 1.34e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2621 TDENkslIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKEsKRQLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQ 2700
Cdd:TIGR02168  184 TREN---LDRLEDILNELERQLKSLERQAEKAERYKELKAE-LRELELALLVLRLEELREELEELQEELKEAEEELEELT 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2701 ALKHQVDLAKRLAQDLVVEASDSKGTSDVLLQveTIAQEHSTLSQQV---DEKCSFLETKLQGIghfQNTIREMFSQFAE 2777
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELY--ALANEISRLEQQKqilRERLANLERQLEEL---EAQLEELESKLDE 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2778 FDDELDSMAPvgrDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLatEETSPDLVGIKRDLEALSKQCNKLLDRA 2857
Cdd:TIGR02168  335 LAEELAELEE---KLEELKEELESLEAELEELEAELEELESRLEELEEQL--ETLRSKVAQLELQIASLNNEIERLEARL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2858 QAREEQVEGTIKRLEEFYSKLKEfsillQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGL 2937
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEE-----AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2938 IQSAAKSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEA--LLHCG-RFQDALE-----SLLSWMVDTEE----LVAN 3005
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLseLISVDeGYEAAIEaalggRLQAVVVENLNaakkAIAF 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3006 QKPPSAEFKVVKA--QIQEQKLLQRLLDDRKStVEVIKREGEKIATTAEPADKV--KILKQLSLLDSRWEAL----LNKA 3077
Cdd:TIGR02168  565 LKQNELGRVTFLPldSIKGTEIQGNDREILKN-IEGFLGVAKDLVKFDPKLRKAlsYLLGGVLVVDDLDNALelakKLRP 643

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3078 ETRNRQLEGISV---------VAQQFHETLEPLNEwlttIEKrlvNCEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQ 3148
Cdd:TIGR02168  644 GYRIVTLDGDLVrpggvitggSAKTNSSILERRRE----IEE---LEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3149 AVSIGQSLKVLSSREDKDmvqskldfsqvwYIEIQEKSHSRSELLQQAlcnakifGEDEVELMNWLNEVHDKLSKLSVQD 3228
Cdd:TIGR02168  717 LRKELEELSRQISALRKD------------LARLEAEVEQLEERIAQL-------SKELTELEAEIEELEERLEEAEEEL 777

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3229 YSTEGLWKQQSELrvlQEDILLRKQNVDQALlNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQL 3308
Cdd:TIGR02168  778 AEAEAEIEELEAQ---IEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3309 ARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEA-----SQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVpwRAR 3383
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEAlallrSELEELSEELRELESKRSELRRELEELREKLAQLE--LRL 931

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3384 EGLEKMVAED----NERYRLVSDTITQKVEEIDAAILRSQQFdqaadaelswITETEKKLMSLGDIRLEQDQTSAQLQVQ 3459
Cdd:TIGR02168  932 EGLEVRIDNLqerlSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKELGPVNLAAIEEYEELKER 1001

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|..
gi 34577049   3460 KTFtmeILRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQ 3511
Cdd:TIGR02168 1002 YDF---LTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFP 1050
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 2085-2757 1.48e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 48.51  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2085 LGLLLKDKIAELNTKLSKLQKAQEessammqwLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQE-- 2162
Cdd:TIGR01612  601 LKLELKEKIKNISDKNEYIKKAID--------LKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEdd 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2163 ---LKDKLTELLEENP--DTPEAPRWKQMLTEIDSKWQELNQLtidrqqKLEESSNNLTQFQTVEAQLKQWLVEkeLMVS 2237
Cdd:TIGR01612  673 idaLYNELSSIVKENAidNTEDKAKLDDLKSKIDKEYDKIQNM------ETATVELHLSNIENKKNELLDIIVE--IKKH 744

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2238 VLGPLSIDPNML----NTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQLS 2313
Cdd:TIGR01612  745 IHGEINKDLNKIledfKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIS 824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2314 DRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAvSTHpdamNQQLETAQKMKQEIQQEK-----KQIKVAQALC 2388
Cdd:TIGR01612  825 IKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKID-SEH----EQFAELTNKIKAEISDDKlndyeKKFNDSKSLI 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2389 EDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHV-----------QHLQSACASSHQFQQMSRDFQAWLDTKKEEQ 2457
Cdd:TIGR01612  900 NEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHnkqnilkeilnKNIDTIKESNLIEKSYKDKFDNTLIDKINEL 979

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2458 NKSHPiSAKLDVLES----LIKDHKDFSKTL-TAQSHMYEKTIAEGE----NLLLKTQGSEKAALQLQL----------- 2517
Cdd:TIGR01612  980 DKAFK-DASLNDYEAknneLIKYFNDLKANLgKNKENMLYHQFDEKEkatnDIEQKIEDANKNIPNIEIaihtsiyniid 1058

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2518 ---NTIKTNWDTFNKQVKERE-------NKLKESL----------EKALKY-------KEQVETLWPWIDKCQNNLEEIK 2570
Cdd:TIGR01612 1059 eieKEIGKNIELLNKEILEEAeinitnfNEIKEKLkhynfddfgkEENIKYadeinkiKDDIKNLDQKIDHHIKALEEIK 1138

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2571 fcldpAEGENSIAKLKSlqkemdqhfgmvellnnTANSLLSVCeiDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQ 2650
Cdd:TIGR01612 1139 -----KKSENYIDEIKA-----------------QINDLEDVA--DKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2651 KFKEFQEVSKEsKRQLQCAKeqlDIHDSLGsQAYSNKYLTMLQTQQ-------KSLQALKHQVDLAKRLAQDLVVEAS-- 2721
Cdd:TIGR01612 1195 LLNEIAEIEKD-KTSLEEVK---GINLSYG-KNLGKLFLEKIDEEKkksehmiKAMEAYIEDLDEIKEKSPEIENEMGie 1269

                          730       740       750
                   ....*....|....*....|....*....|....*..
gi 34577049   2722 -DSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETK 2757
Cdd:TIGR01612 1270 mDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK 1306
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2869-2977 1.84e-04

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: 43.85  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2869 KRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTq 2948
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE- 77

                           90       100
                   ....*....|....*....|....*....
gi 34577049   2949 gLEHDLDDVNARWKTLNKKVAQRAAQLQE 2977
Cdd:pfam00435   78 -IQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 375-469 1.91e-04

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: 43.85  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    375 LHNFVSRATNELIWLNEKEE----EEVAYDWSErntnIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTI 450
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                           90
                   ....*....|....*....
gi 34577049    451 EAYRAAMQTQWSWILQLCQ 469
Cdd:pfam00435   79 QERLEELNERWEQLLELAA 97
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 4187-4289 1.95e-04

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: 43.85  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4187 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYfSQKQDVVLIKNLL 4266
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|...
gi 34577049   4267 ISVQSRWEKVVQRLVERGRSLDD 4289
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 2398-3082 1.96e-04

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: 48.19  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2398 EYLKAELSRQLEGILKSFKD-VEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEE-QNKSHPISAKLDVLESLIK 2475
Cdd:pfam15921  248 EALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQaRNQNSMYMRQLSDLESTVS 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2476 DhkdFSKTLTAQSHMYEKTIAEGENLLLKTQGsekaalqlQLNTIKTNWDTFNKQVKERENKLKESL------EKALKY- 2548
Cdd:pfam15921  328 Q---LRSELREAKRMYEDKIEELEKQLVLANS--------ELTEARTERDQFSQESGNLDDQLQKLLadlhkrEKELSLe 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2549 KEQVETLWPWIDKCQNNLEEIKFCLDP--AEGENSIAKLKSLQKE----MDQHFGMVELLNNtanSLLSVCEIDKEVvtD 2622
Cdd:pfam15921  397 KEQNKRLWDRDTGNSITIDHLRRELDDrnMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNE---SLEKVSSLTAQL--E 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2623 ENKSLIQKVdmvTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLdihdslgsqaysNKYLTMLQTQQKSLQAL 2702
Cdd:pfam15921  472 STKEMLRKV---VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI------------TKLRSRVDLKLQELQHL 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2703 KHQVDLAKRLAQD---LVVEASDSKGTSDVL-LQVETIAQ--------------EHSTLSQQV-DEKCSFLETKLQGiGH 2763
Cdd:pfam15921  537 KNEGDHLRNVQTEceaLKLQMAEKDKVIEILrQQIENMTQlvgqhgrtagamqvEKAQLEKEInDRRLELQEFKILK-DK 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2764 FQNTIREMFSQFAefDDELDSMAPVGRDAETLQkqkeTIKAFLKKLEALMasndNANKTCKMMLatEETSPDLVGIKRDL 2843
Cdd:pfam15921  616 KDAKIRELEARVS--DLELEKVKLVNAGSERLR----AVKDIKQERDQLL----NEVKTSRNEL--NSLSEDYEVLKRNF 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2844 ----EALSKQCNKL---LDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQ-GPVGMETETINQQL---NMF 2912
Cdd:pfam15921  684 rnksEEMETTTNKLkmqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQiDALQSKIQFLEEAMtnaNKE 763

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2913 KVFQKEEieplqgkqqdVNWLGQGLIQSAAKSTSTQGlehDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDAL--- 2989
Cdd:pfam15921  764 KHFLKEE----------KNKLSQELSTVATEKNKMAG---ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIqrq 830

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2990 --ESL---LSWMVDTEELvanQKPPSAEFKVVKAQIQEQKLLQRL---LDDRKSTVEVIKREGEKiaTTAEPADKVKILK 3061
Cdd:pfam15921  831 eqESVrlkLQHTLDVKEL---QGPGYTSNSSMKPRLLQPASFTRThsnVPSSQSTASFLSHHSRK--TNALKEDPTRDLK 905

                          730       740
                   ....*....|....*....|....*.
gi 34577049   3062 QL-----SLLDSRWEALLNKAETRNR 3082
Cdd:pfam15921  906 QLlqelrSVINEEPTVQLSKAEDKGR 931
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 745-943 2.53e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    745 EVRNIRLRLENC---EDRLIRQIRTPLERddlhESVFRiTEQEKLKKELERLKDDLGTITNKCEE-FFSQAAASSSVPTL 820
Cdd:pfam05483  514 ELKKHQEDIINCkkqEERMLKQIENLEEK----EMNLR-DELESVREEFIQKGDEVKCKLDKSEEnARSIEYEVLKKEKQ 588

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    821 RSELNVVLQNMNQVYSMSSTYIDKLKTVNLVLKNTQAAEA-LVKLYETKLCEEEAVIAD-KNNIENLISTlkqWRSEVDE 898
Cdd:pfam05483  589 MKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASaKQKFEEIIDN---YQKEIED 665

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 34577049    899 KRQVFHALEDELQKAKAISDEMFKTYKERDLD-----------FDWHKEKADQLVE 943
Cdd:pfam05483  666 KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalMEKHKHQYDKIIE 721
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1751-1958 2.98e-04

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: 45.51  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1751 QDGLDEMLDWMGNVESSLKEQgQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEtTDPSTASSLQAKMKD 1830
Cdd:cd00176    6 LRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERLEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 1831 LSARFSEASHKHKETLAKMEELKTKVELFENLSEkLQTFLETKTQALTEVDVPG--KDVTELSQYMQESTSEFLEHKKHL 1908
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEPRL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 34577049 1909 EVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSC 1958
Cdd:cd00176  163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
3637-3741 3.06e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.09  E-value: 3.06e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3637 QFHDKIDQILESLERiVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGtdkdiSAKAV 3716
Cdd:smart00150    2 QFLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEI 75

                            90       100
                    ....*....|....*....|....*
gi 34577049    3717 QDKLDQMVFIWENIHTLVEEREAKL 3741
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKL 100
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2140-2728 3.45e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2140 KTQVEQNKSFEAELKQNVNKVQELKDK-LTELLEEnpdtpeaprwKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQF 2218
Cdd:TIGR04523  116 KEQKNKLEVELNKLEKQKKENKKNIDKfLTEIKKK----------EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2219 QTVEAQLKQWLVEKELMVSVLGPLSIDPNMLNTQ----RQQVQILLQEFATRKPQYEQLTAagqgILSRpgedpslrgiV 2294
Cdd:TIGR04523  186 QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiselKKQNNQLKDNIEKKQQEINEKTT----EISN----------T 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2295 KEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQ--QLETAQ---- 2368
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQekKLEEIQnqis 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2369 -------KMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAE-LSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQ 2440
Cdd:TIGR04523  332 qnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEkLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2441 QMSRDFQAWLDTKKEEQNKshpisakldvLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLlKTQGSEKAALQLQLNTI 2520
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKI 480

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2521 KTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKfcLDPAEGENSIAKLKSLQKEMDQhfgmve 2600
Cdd:TIGR04523  481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLEDELNKDDF------ 552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2601 llNNTANSL-LSVCEIDKEVVT--DENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQldiHD 2677
Cdd:TIGR04523  553 --ELKKENLeKEIDEKNKEIEElkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE---NE 627

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 34577049   2678 SLGSQAysNKYLTMLQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGTSD 2728
Cdd:TIGR04523  628 KLSSII--KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1932-2673 3.56e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1932 EKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVpivqpsFGAEDLGKSLEDTKKLQEKwSL 2011
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL------YALANEISRLEQQKQILRE-RL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2012 KTPEIQKVNNSGiSLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEefwaNKGLTSIKKDMTDISHGYEDLGLLLKD 2091
Cdd:TIGR02168  312 ANLERQLEELEA-QLEELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRS 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2092 KIAELNTKLSKLQKAQEESSAMMQWLQKMNKtatKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELL 2171
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRE---RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2172 EEnpdtpEAPRWKQMLTEIDSKWQELNQLTiDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPL-SIDP---- 2246
Cdd:TIGR02168  464 EE-----LREELEEAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEgyea 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2247 ---------------NMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQ 2311
Cdd:TIGR02168  538 aieaalggrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2312 LSDR------CDWIDQAIVKSTQYQSLLRSLSdklsdLDNKLSSSLAVST--HPDAMNQQLETaqkmKQEIQQEKKQIKV 2383
Cdd:TIGR02168  618 LSYLlggvlvVDDLDNALELAKKLRPGYRIVT-----LDGDLVRPGGVITggSAKTNSSILER----RREIEELEEKIEE 688

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2384 AQALCEDLSALVkeeylkAELSRQLEGILKSFKDVEQKAEnhvqhlqsacasshqfqQMSRDFQAWLDTKKEEQNKSHPI 2463
Cdd:TIGR02168  689 LEEKIAELEKAL------AELRKELEELEEELEQLRKELE-----------------ELSRQISALRKDLARLEAEVEQL 745

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2464 SAKLDVLESLIKDhkdfsktLTAQSHMYEKTIAEgENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLE 2543
Cdd:TIGR02168  746 EERIAQLSKELTE-------LEAEIEELEERLEE-AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2544 KALKYKEQVETLWPWIDKCQNNLEEIKfcldpAEGENSIAKLKSLQKEMDQhfgmvellnntansllsvCEIDKEVVTDE 2623
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLE-----EQIEELSEDIESLAAEIEE------------------LEELIEELESE 874

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 34577049   2624 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQL 2673
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3859-3961 3.66e-04

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: 43.08  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3859 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 3938
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81

                           90       100
                   ....*....|....*....|...
gi 34577049   3939 LMELKLIWDSLEERIINRQHKLE 3961
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1177-2021 3.94e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1177 GDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSGDVKVEEKIVAERQQEYKEKLqgicDLLTQTENRLIGHQE 1256
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----YLLYLDYLKLNEERI 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1257 AFMIGDGTVELKKYQSKQEELQKDMQGSAQALAE------VVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNL 1330
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1331 KAEQSK--KELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKqvieqngthfQEGDGKSAI 1408
Cdd:pfam02463  320 EKEKKKaeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK----------LESERLSSA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1409 GEEDEVNGNLLETDVDgQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYlspEEKEKLQKNMKEL 1488
Cdd:pfam02463  390 AKLKEEELELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---LEKQELKLLKDEL 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1489 KVHYETALAESEKKMKLTHSLQEELEKFDADytEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDL 1568
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLE--ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1569 RYITISGNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGL 1648
Cdd:pfam02463  544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1649 QACeataskhlsepiaVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYED 1728
Cdd:pfam02463  624 VVE-------------GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1729 LSKSVNERNEKLQITLTRSLSVQDGLDEMLdwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEK 1808
Cdd:pfam02463  691 KEEILRRQLEIKKKEQREKEELKKLKLEAE-----------------ELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1809 VKKFMETTDPSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVT 1888
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1889 ELSQYMQESTSEFLEHKKHLEVLHSLLKEISSHGLPSDKALVLEKtnnlSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVL 1968
Cdd:pfam02463  834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE----LEEQKLKDELESKEEKEKEEKKELEEESQKL 909

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|...
gi 34577049   1969 VKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNN 2021
Cdd:pfam02463  910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 785-2031 4.17e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.35  E-value: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    785 KLKKELERLKDDLGTITNKCEEFFSQAAASSS----VPTLRSELNVVLQNMnqvySMSSTYIDKLKTVNLVLKNTQAaea 860
Cdd:TIGR01612  562 EIKKELEEENEDSIHLEKEIKDLFDKYLEIDDeiiyINKLKLELKEKIKNI----SDKNEYIKKAIDLKKIIENNNA--- 634

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    861 lvklyetkLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFhalEDELQKakaISDEMFKTYKERDLDFDWHKEKADQ 940
Cdd:TIGR01612  635 --------YIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIY---EDDIDA---LYNELSSIVKENAIDNTEDKAKLDD 700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    941 LVERWQNVHVQIDNrlRDLEGIGKSLKYYRDTYHPLDDWIqqVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQS 1020
Cdd:TIGR01612  701 LKSKIDKEYDKIQN--METATVELHLSNIENKKNELLDII--VEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1021 KMDECQKYAEQYSATVKDYELQTmtyraMVDSQQKSPVKRRRMQSsadliiQEFMDLRTRYTALVTLMTQYIKFAGDSLk 1100
Cdd:TIGR01612  777 EKDELNKYKSKISEIKNHYNDQI-----NIDNIKDEDAKQNYDKS------KEYIKTISIKEDEIFKIINEMKFMKDDF- 844

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1101 rleeeeksleeekkehvekAKELQKWVsNISKTLKDAEKAGKPPFS------KQKISSEEISTKKEQLSEALQTIqlfla 1174
Cdd:TIGR01612  845 -------------------LNKVDKFI-NFENNCKEKIDSEHEQFAeltnkiKAEISDDKLNDYEKKFNDSKSLI----- 899

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1175 khgdkmtDEERNELEKQ---VKTLQESYNLL-----FSESLKQLQESQTSGDVKVEEKIVAERQQEYKEKlqgicDLLTQ 1246
Cdd:TIGR01612  900 -------NEINKSIEEEyqnINTLKKVDEYIkicenTKESIEKFHNKQNILKEILNKNIDTIKESNLIEK-----SYKDK 967

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1247 TENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAevvKNTENFLKengEKLSQEDKAL--IEQKLNEAKik 1324
Cdd:TIGR01612  968 FDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLG---KNKENMLY---HQFDEKEKATndIEQKIEDAN-- 1039

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1325 ceqlnlkaeQSKKELDKVVTTAIKEETEkvaavkqleesktKIENLldwlsnVDKDSERAGTKHKQVIEQNGTHFQEGDG 1404
Cdd:TIGR01612 1040 ---------KNIPNIEIAIHTSIYNIID-------------EIEKE------IGKNIELLNKEILEEAEINITNFNEIKE 1091

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1405 KSAIGEEDEV--NGNLLETDVDGQVGTTQENLNQQYQK-------VKAQHEKIISQHQAVI----------IATQSAQVL 1465
Cdd:TIGR01612 1092 KLKHYNFDDFgkEENIKYADEINKIKDDIKNLDQKIDHhikaleeIKKKSENYIDEIKAQIndledvadkaISNDDPEEI 1171

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1466 LEKQGQYLSPEEKEK-LQKNMKEL-----KVHYETALAESEKKMKLTH--SLQEE-LEKFDADYTEFEHWLQQSEQELEN 1536
Cdd:TIGR01612 1172 EKKIENIVTKIDKKKnIYDEIKKLlneiaEIEKDKTSLEEVKGINLSYgkNLGKLfLEKIDEEKKKSEHMIKAMEAYIED 1251

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1537 L----EAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNR------VLEAAKSCSKRDGGKVDTSATHREVQRKL 1606
Cdd:TIGR01612 1252 LdeikEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHdenisdIREKSLKIIEDFSEESDINDIKKELQKNL 1331

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1607 ----DHATDRFRSLYSKCNVLG----NNLKDLVDKYQHY----EDASCGLLAGLQACEaTASKHLSEPIA---------- 1664
Cdd:TIGR01612 1332 ldaqKHNSDINLYLNEIANIYNilklNKIKKIIDEVKEYtkeiEENNKNIKDELDKSE-KLIKKIKDDINleeckskies 1410

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1665 -VDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAE-----VLLDARgSLLPAKNDIQKTLDDIVGR-YEDLSKSVNERN 1737
Cdd:TIGR01612 1411 tLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADennenVLLLFK-NIEMADNKSQHILKIKKDNaTNDHDFNINELK 1489

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1738 EKLQitltRSLSVQDGLD---EMLDWMGNVESSLKEQGQVPLNSTALQDIISKNIMLEQDiagRQSSINAMNEKVKKFme 1814
Cdd:TIGR01612 1490 EHID----KSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKD---SEIIIKEIKDAHKKF-- 1560

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1815 TTDPSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYM 1894
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDS 1640

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1895 QEstSEFLEHKKHLEVLHSLLKEISSHglpsDKALVLEKT--NNLSKKFKEMEDTIKEKKE-----AVTSCQEQLDAFQV 1967
Cdd:TIGR01612 1641 QD--TELKENGDNLNSLQEFLESLKDQ----KKNIEDKKKelDELDSEIEKIEIDVDQHKKnyeigIIEKIKEIAIANKE 1714

                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34577049   1968 LVKSLKSWIKETTKKvpiVQPSFGAEDLgKSLEDTKKLQEkwslKTPEIQKVNNSGISLCNLIS 2031
Cdd:TIGR01612 1715 EIESIKELIEPTIEN---LISSFNTNDL-EGIDPNEKLEE----YNTEIGDIYEEFIELYNIIA 1770
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 4790-4862 4.50e-04

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: 44.17  E-value: 4.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34577049 4790 VMDFFRRIDKDQDGKIT----RQEFIDGILSSKFP-TSRLEMSavadIFDRDGDGYIDYYEFvAALhpnkdaYKPITD 4862
Cdd:cd16183    2 LWNVFQRVDKDRSGQISatelQQALSNGTWTPFNPeTVRLMIG----MFDRDNSGTINFQEF-AAL------WKYITD 68
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 2335-3306 4.71e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.96  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2335 SLSDKLSDLDNKLSSSLAVS---------THPDAMNQQLETAQKMKQ---EIQQEKKQIKvAQALCEDLSALVKEEYLKA 2402
Cdd:TIGR00606  127 SLSSKCAEIDREMISHLGVSkavlnnvifCHQEDSNWPLSEGKALKQkfdEIFSATRYIK-ALETLRQVRQTQGQKVQEH 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2403 ELSRQLegiLKSFKDVEQKAENHVQHLQSACASShqfQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFSK 2482
Cdd:TIGR00606  206 QMELKY---LKQYKEKACEIRDQITSKEAQLESS---REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2483 TLTAQSHMYE--------------KTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKY 2548
Cdd:TIGR00606  280 QMEKDNSELElkmekvfqgtdeqlNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2549 KEQVETLWPWIDKCQNNLEEIKFCLDPaEGENSIAKLKSLQKE-MDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSL 2627
Cdd:TIGR00606  360 QEHIRARDSLIQSLATRLELDGFERGP-FSERQIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGL 438

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2628 IQKVDMVTEQLHSKKfclENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLgSQAYSNKYLTMLQTQQKSLQALKHQVD 2707
Cdd:TIGR00606  439 GRTIELKKEILEKKQ---EELKFVIKELQQLEGSSDRILELDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNEKADLD 514

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2708 LAKRlAQDLVVEASDSKGTSdvLLQVETIAQEHSTLSQQVDEKCSFLETKLQG-IGHFQNTI---REMFSQFAEFDDELD 2783
Cdd:TIGR00606  515 RKLR-KLDQEMEQLNHHTTT--RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSlLGYFPNKKqleDWLHSKSKEINQTRD 591

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2784 SMAPVGRDAETLQKQKETIKAFLKKLEALMAS-NDNANKTCkmmlATEETSPDLVGIKRDLEALSKQ------------- 2849
Cdd:TIGR00606  592 RLAKLNKELASLEQNKNHINNELESKEEQLSSyEDKLFDVC----GSQDEESDLERLKEEIEKSSKQramlagatavysq 667

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2850 -----------CNKLLDRAQAREEQVEGTIKRLEE----FYSKLKEFSILLQKAE-EHEESQGPVGMETETINQqlnmfk 2913
Cdd:TIGR00606  668 fitqltdenqsCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDL------ 741

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2914 vfQKEEIEPLQGKQQDVNwlgqgliqsaaksTSTQGLEHDLDDVNARWKTLNKKVaQRAAQLQEALLHCGRFQDALE--- 2990
Cdd:TIGR00606  742 --KEKEIPELRNKLQKVN-------------RDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKdve 805

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2991 --------SLLSWMVDTEELVANQKPPSAEFKVVKAqIQEQKLLQRLLDDRKSTVEVIKREGEKIATtaepaDKVKILKQ 3062
Cdd:TIGR00606  806 rkiaqqaaKLQGSDLDRTVQQVNQEKQEKQHELDTV-VSKIELNRKLIQDQQEQIQHLKSKTNELKS-----EKLQIGTN 879

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3063 LslldSRWEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTIEKRlvNCEPIG---TQASKLEEQIAQHKALEDDI 3139
Cdd:TIGR00606  880 L----QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISskeTSNKKAQDKVNDIKEKVKNI 953

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3140 INHNKHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQE----------KSHSRSELLQQALCNAKIfgEDEVE 3209
Cdd:TIGR00606  954 HGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEdmrlmrqdidTQKIQERWLQDNLTLRKR--ENELK 1031

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3210 LMNWLNEVHDKlsklsvqDYSTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYK 3289
Cdd:TIGR00606 1032 EVEEELKQHLK-------EMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104

                         1050      1060
                   ....*....|....*....|....*..
gi 34577049   3290 D------ITKLS----TDVAKTLEQAL 3306
Cdd:TIGR00606 1105 EmmivmrTTELVnkdlDIYYKTLDQAI 1131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3310-4196 4.99e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3310 RRLHSTHEELctwlDKVEVELLSYETQVLK-GEEASQAQmRPKELKKEAKNNKALLdSLNEVSSALLELvpwRAREGLEK 3388
Cdd:TIGR02168  179 RKLERTRENL----DRLEDILNELERQLKSlERQAEKAE-RYKELKAELRELELAL-LVLRLEELREEL---EELQEELK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3389 MVAEDNERYRLVSDTITQKVEEIDAAIL-RSQQFDQAADAELSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEIL 3467
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSeLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3468 RHKDI-IDDLVKSGHKIMTAcsEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERAQSLVNQFWETYEELwpwLTETQS 3546
Cdd:TIGR02168  330 SKLDElAEELAELEEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIER 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3547 IISQLPAPALEYETLRQQQEEHRQlreliaehKPHIDKMNKTGPQLLELSPGEgFSIQEKYVAADTLYSQIKEDVKKRAV 3626
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLK--------KLEEAELKELQAELEELEEEL-EELQEELERLEEALEELREELEEAEQ 475

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3627 ALDEAISQstqfHDKIDQILESLERIVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETlkqrgeEMIARSGG 3706
Cdd:TIGR02168  476 ALDAAERE----LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEA------AIEAALGG 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3707 TDKDIsakaVQDKLDQmvfIWENIHTLVEEREAKLLdVMEL----AEKFWCDHMSLIVTIKDTQDFIRDLE--DPGIDPS 3780
Cdd:TIGR02168  546 RLQAV----VVENLNA---AKKAIAFLKQNELGRVT-FLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVkfDPKLRKA 617

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3781 ---------VVKQQQEAAETIREeidgLQEELDIVInLGSELIAACGEpdkpIVKKSIDELNSAwdsLNKawKDRIDKLE 3851
Cdd:TIGR02168  618 lsyllggvlVVDDLDNALELAKK----LRPGYRIVT-LDGDLVRPGGV----ITGGSAKTNSSI---LER--RREIEELE 683

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3852 EAM-QAAVQYQDGLQAvfdwvdiaggklasmspigtdLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEES 3930
Cdd:TIGR02168  684 EKIeELEEKIAELEKA---------------------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3931 DKHTVQdplmelkliWDSLEERIINRQHKLEGALLALGQFQHALDELLawlthtEGLLSEQKPVGGdpkaieielakhhv 4010
Cdd:TIGR02168  743 EQLEER---------IAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQ-------------- 793

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4011 LQNDVLAHQSTVEAVNKAGNDLiessaGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQQWL 4090
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLL-----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   4091 TDTER---HLLASKplgglpETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCpksaetniDQDINNLKEKWESV 4167
Cdd:TIGR02168  869 EELESeleALLNER------ASLEEALALLRSELEELSEELRELESKRSELRRELEEL--------REKLAQLELRLEGL 934

                          890       900
                   ....*....|....*....|....*....
gi 34577049   4168 ETKLNERKTKLEEALNLAMEFHNSLQDFI 4196
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENKI 963
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 4793-4851 5.46e-04

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: 43.74  E-value: 5.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34577049 4793 FFRRIDKDQDGKITRQEfIDGILSSkfptSRLEMS-AVAD----IFDRDGDGYIDYYEFvAALH 4851
Cdd:cd16185    5 WFRAVDRDRSGSIDVNE-LQKALAG----GGLLFSlATAEklirMFDRDGNGTIDFEEF-AALH 62
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 1200-2682 5.68e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 46.58  E-value: 5.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1200 NLLFSESLKQLQESQTSGDVKVEEKIVAerQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQS------- 1272
Cdd:TIGR01612 1106 NIKYADEINKIKDDIKNLDQKIDHHIKA--LEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtkid 1183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1273 KQEELQKDMQGSAQALAEVVKNTENFLKENGEKLS--QEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKvvttaIKEE 1350
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSygKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDE-----IKEK 1258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1351 TEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIeqngthfqegdgkSAIGEEDE--VNGNLLETDVDGQVG 1428
Cdd:TIGR01612 1259 SPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENI-------------SDIREKSLkiIEDFSEESDINDIKK 1325

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1429 TTQENLNQQyQKVKAQHEKIISQHQAV--IIATQSAQVLLEKQGQYlsPEEKEKLQKNMKELKVHYETALaeseKKMKLT 1506
Cdd:TIGR01612 1326 ELQKNLLDA-QKHNSDINLYLNEIANIynILKLNKIKKIIDEVKEY--TKEIEENNKNIKDELDKSEKLI----KKIKDD 1398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1507 HSLQEELEKFDA--DYTEFEHWLQQSEQELENLEAGADDINglmTKLKRQKSFSEDVIShkgDLRYITISGNRVLEAAKS 1584
Cdd:TIGR01612 1399 INLEECKSKIEStlDDKDIDECIKKIKELKNHILSEESNID---TYFKNADENNENVLL---LFKNIEMADNKSQHILKI 1472

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1585 csKRDGGKVDTSATHREVQRKLDHAtdrfrslySKCNVLGNNLKDLVDK----YQHYEDASCGLLAGLQACEA----TAS 1656
Cdd:TIGR01612 1473 --KKDNATNDHDFNINELKEHIDKS--------KGCKDEADKNAKAIEKnkelFEQYKKDVTELLNKYSALAIknkfAKT 1542

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1657 KHLSEPIAVDPKNLQRQ--LEETKALQ--GQISSQQVAVE----KLKKTAEVLLDARGSLLPAKN------DIQKTLDDI 1722
Cdd:TIGR01612 1543 KKDSEIIIKEIKDAHKKfiLEAEKSEQkiKEIKKEKFRIEddaaKNDKSNKAAIDIQLSLENFENkflkisDIKKKINDC 1622

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1723 VGRYEDLSK-----SVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKEqgqvplnstaLQDIISKNIMLEQDIAG 1797
Cdd:TIGR01612 1623 LKETESIEKkissfSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE----------LDELDSEIEKIEIDVDQ 1692

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1798 RQSSIN-AMNEKVKKFMETTD---PSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKV----ELFENLSEKLQTF 1869
Cdd:TIGR01612 1693 HKKNYEiGIIEKIKEIAIANKeeiESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIgdiyEEFIELYNIIAGC 1772

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1870 LET-KTQALTEVDVPGKDVTELSQYMQESTSEflehKKHLEVLHSL----LKEISSHgLPSDKALVLEKTNNLSKKFKEM 1944
Cdd:TIGR01612 1773 LETvSKEPITYDEIKNTRINAQNEFLKIIEIE----KKSKSYLDDIeakeFDRIINH-FKKKLDHVNDKFTKEYSKINEG 1847

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1945 EDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVpiVQPSFGAEDLGKSLedtKKLqeKWSLKtpeIQKVNNSGI 2024
Cdd:TIGR01612 1848 FDDISKSIENVKNSTDENLLFDILNKTKDAYAGIIGKKY--YSYKDEAEKIFINI---SKL--ANSIN---IQIQNNSGI 1917

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2025 SLCNLISavttpakaIAAVKSggavLNGEgtATNTEEFWANKGLTSikKDMTDISHGYedlglllkdkiaelNTKLSKLQ 2104
Cdd:TIGR01612 1918 DLFDNIN--------IAILSS----LDSE--KEDTLKFIPSPEKEP--EIYTKIRDSY--------------DTLLDIFK 1967

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2105 KAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKsfeaelKQNVNKVQELKDKLTELLE-----ENPDTP- 2178
Cdd:TIGR01612 1968 KSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKYKK------EKILNDVKLLLHKFDELNKlscdsQNYDTIl 2041

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2179 EAPRWKQMLTEIDSKWQELNQLTIDRQQKLEES--SNNLTQFQTVEAQLKQWLVEKElmvsvlgPLSIDPNMLNTQRQQV 2256
Cdd:TIGR01612 2042 ELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEkfDNDIKDIEKFENNYKHSEKDNH-------DFSEEKDNIIQSKKKL 2114

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2257 QILLQEFATRKPQYEQLTAAGQGILSRpgedpsLRGIVKE-QLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQYQSLLRS 2335
Cdd:TIGR01612 2115 KELTEAFNTEIKIIEDKIIEKNDLIDK------LIEMRKEcLLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIED 2188

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2336 LSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQE-IQQEKKQIKVAQALCE---------DLSAL----VKEEYLK 2401
Cdd:TIGR01612 2189 ISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNlIEKEKEATKIINNLTElftidfnnaDADILhnnkIQIIYFN 2268

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2402 AELSRQLEGILKSFKDVEQKAENHVQHLQSacasshQFQQMSRDFQAWLDTKKeeqNKSHPISAKLDVLESLIKDHKD-F 2480
Cdd:TIGR01612 2269 SELHKSIESIKKLYKKINAFKLLNISHINE------KYFDISKEFDNIIQLQK---HKLTENLNDLKEIDQYISDKKNiF 2339

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2481 SKTLTAQSHMYEKTIAEGENLLLKTQGsekaalqlQLNTIKtnwdtfNKQVKERENkLKESLEKALKYKEQVETLWPWID 2560
Cdd:TIGR01612 2340 LHALNENTNFNFNALKEIYDDIINREN--------KADEIE------NINNKENEN-IMQYIDTITKLTEKIQDILIFVT 2404

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2561 KCQNNLEEIKFCLDPAEgENSIAKLKSLQKEMDQHFGmvELLNNtansllsVCEIDKEVVTDENKSLI-----QKVDMVt 2635
Cdd:TIGR01612 2405 TYENDNNIIKQHIQDND-ENDVSKIKDNLKKTIQSFQ--EILNK-------IDEIKAQFYGGNNINNIiitisQNANDV- 2473

                         1530      1540      1550      1560      1570
                   ....*....|....*....|....*....|....*....|....*....|
gi 34577049   2636 EQLHSKKFCLEN-MTQKFKEFQEV--SKESKRQLQCAKEQLDIHDSLGSQ 2682
Cdd:TIGR01612 2474 KNHFSKDLTIENeLIQIQKRLEDIknAAHEIRSEQITKYTNAIHNHIEEQ 2523
PTZ00121 PTZ00121
MAEBL; Provisional
 858-1517 6.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   858 AEALVKLYETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALE-----DELQKAKAI--SDEMFKTYKERDLD 930
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkaDELKKAEEKkkADEAKKAEEKKKAD 1305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   931 ------------------FDWHKEKADQLVERWQNVHVQIDNRLRDLEGIGKSLKYYRDTYHP----LDDWIQQVETTQR 988
Cdd:PTZ00121 1306 eakkkaeeakkadeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkKEEAKKKADAAKK 1385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   989 KIQE-NQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSatvKDYELQTMTYRAMVDSQQKSPVKRRRMQSSA 1067
Cdd:PTZ00121 1386 KAEEkKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1068 DLIIQEFMDL-RTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTLKDAEKAGKPPFS 1146
Cdd:PTZ00121 1463 KKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1147 KQKISSEEIStKKEQLSEALQTIQLFLAKHG--DKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSgdvKVEEK 1224
Cdd:PTZ00121 1543 EEKKKADELK-KAEELKKAEEKKKAEEAKKAeeDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK---KAEEA 1618

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1225 IVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQ--SKQEELQKDMQGSAQALAEVVKNTENFLKEN 1302
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1303 GEKLSQEDkalIEQKLNEAKIKCEQL-------NLKAEQSKKELDkvvttaikEETEKVAAVKQLEESKTKIENLldwLS 1375
Cdd:PTZ00121 1699 EEAKKAEE---LKKKEAEEKKKAEELkkaeeenKIKAEEAKKEAE--------EDKKKAEEAKKDEEEKKKIAHL---KK 1764

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1376 NVDKDSERAGTKHKQVIEQNgthFQEGDGKSAIGEEDEVNgnlletDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAV 1455
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIK------DIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049  1456 IIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFD 1517
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD 1897
SPEC smart00150
Spectrin repeats;
3092-3194 6.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 6.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    3092 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLkVLSSREDKDMVQSK 3171
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEER 78

                            90       100
                    ....*....|....*....|...
gi 34577049    3172 LDFSQVWYIEIQEKSHSRSELLQ 3194
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
EF-hand_8 pfam13833
EF-hand domain pair;
4801-4850 6.83e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 40.38  E-value: 6.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 34577049   4801 QDGKITRQEFIDGI-LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 4850
Cdd:pfam13833    1 EKGVITREELKRALaLLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1476-2008 6.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1476 EEKEKLQKNMKELKVHYEtalaESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEagaddinglmTKLKRQK 1555
Cdd:PRK03918  221 EELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----------EKVKELK 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1556 SFSEDVishkgdLRYITISGNRVlEAAKSCSKRDGGKVDTSATHREVQRKLDHATD---RFRSLYSKCNVLGNNLKDLVD 1632
Cdd:PRK03918  287 ELKEKA------EEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1633 KYQHYEDAScGLLAGLQACEATASKHLSEPIAVDPKNLQRQLEETK-----------ALQGQISSQQVAVEKLKKT---- 1697
Cdd:PRK03918  360 RHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEeeiskitarigELKKEIKELKKAIEELKKAkgkc 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1698 ----AEVLLDARGSLLPAK----NDIQKTLDDIVGRYEDLSKsvneRNEKLQITLTRSLSVQDgLDEMLDWMGNVESSLK 1769
Cdd:PRK03918  439 pvcgRELTEEHRKELLEEYtaelKRIEKELKEIEEKERKLRK----ELRELEKVLKKESELIK-LKELAEQLKELEEKLK 513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1770 EQGQVPL--NSTALQDIISKNIMLEQDIAGRQSSINAMNEkvkkfmettdpstassLQAKMKDLSARFSEASHKHKETLA 1847
Cdd:PRK03918  514 KYNLEELekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----------------LKKKLAELEKKLDELEEELAELLK 577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1848 KMEELKtkVELFENLSEKLQTFLETKTQALTEVDVPgKDVTELSQYMQESTSEFLEHKKHLEVLHSLLKEISSHGLPSDK 1927
Cdd:PRK03918  578 ELEELG--FESVEELEERLKELEPFYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1928 ALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVqpsfgaEDLGKSLEDTKKLQE 2007
Cdd:PRK03918  655 KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL------EKLEKALERVEELRE 728


                  .
gi 34577049  2008 K 2008
Cdd:PRK03918  729 K 729
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 4794-4851 1.12e-03

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 44.58  E-value: 1.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049 4794 FRRIDKDQDGKITRQEFIDGILSSKFPTSR-LEMSAVADIFDRDGDGYIDYYEFVAALH 4851
Cdd:cd16230  129 FRVADQDGDSMATREELTAFLHPEEFPHMRdIVVAETLEDLDKNKDGYVQVEEYIADLY 187
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 4789-4851 1.21e-03

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: 42.90  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4789 RVMDFFRRIDKDQDGKITRQEF-------------IDGI--LSSKFPTSR----------------LEMSAVADIFDRDG 4837
Cdd:cd16180    1 ELRRIFQAVDRDRSGRISAKELqralsngdwtpfsIETVrlMINMFDRDRsgtinfdefvglwkyiQDWRRLFRRFDRDR 80

                         90
                 ....*....|....
gi 34577049 4838 DGYIDYYEFVAALH 4851
Cdd:cd16180   81 SGSIDFNELQNALS 94
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4763-4814 1.54e-03

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: 39.84  E-value: 1.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34577049 4763 ELRE-FANFDFD----IWRKKYMRWMNH-----KKSRVMDFFRRIDKDQDGKITRQEFIDGI 4814
Cdd:cd00051    1 ELREaFRLFDKDgdgtISADELKAALKSlgeglSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
SPEC smart00150
Spectrin repeats;
2872-2976 1.66e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 1.66e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2872 EEFYSKLKEFSILLQKAEEHEESQgPVGMETETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqgLE 2951
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAE-LEAHEERVEALNELGEQLIEEGHPDAEE--IE 76

                            90       100
                    ....*....|....*....|....*
gi 34577049    2952 HDLDDVNARWKTLNKKVAQRAAQLQ 2976
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 3008-3584 1.69e-03

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: 45.11  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3008 PPSAEFKVVKAQIQEQklLQRLLDDRKSTVEVIKREGE-KIATTAEPADKVKilKQLSLLDSRWEALLNKAETRN----R 3082
Cdd:pfam15921  242 PVEDQLEALKSESQNK--IELLLQQHQDRIEQLISEHEvEITGLTEKASSAR--SQANSIQSQLEIIQEQARNQNsmymR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3083 QLEGI-SVVAQ---QFHETLEPLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHKALEDDIIN------HNKHLHQAVSI 3152
Cdd:pfam15921  318 QLSDLeSTVSQlrsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlHKREKELSLEK 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3153 GQSlKVLSSREDK-----DMVQSKLDFSQvwyIEIQekshsRSELLQQAL---CNAKIfgEDEVELMNWLNEVHDKLSKL 3224
Cdd:pfam15921  398 EQN-KRLWDRDTGnsitiDHLRRELDDRN---MEVQ-----RLEALLKAMkseCQGQM--ERQMAAIQGKNESLEKVSSL 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3225 SVQDYSTEGLwkqqseLRVLQEDILLRKQNvdqallngLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQ 3304
Cdd:pfam15921  467 TAQLESTKEM------LRKVVEELTAKKMT--------LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3305 ALQLA------RRLHSTHEEL---CTWLDKVeVELLSYE----TQVL--KGEEASQAQMRPKELKKEAKNNKALLDSL-- 3367
Cdd:pfam15921  533 LQHLKnegdhlRNVQTECEALklqMAEKDKV-IEILRQQienmTQLVgqHGRTAGAMQVEKAQLEKEINDRRLELQEFki 611

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3368 --NEVSSALLELVPWRAREGLE--KMVAEDNERYRLVSDtITQKVEEIDAAILRSQQfdqaadaELSWITETEKKLM-SL 3442
Cdd:pfam15921  612 lkDKKDAKIRELEARVSDLELEkvKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRN-------ELNSLSEDYEVLKrNF 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3443 GDIRLEQDQTSAQLQVQ-KTFTMEILRHKDIIDDLVKS-GHKIMTACSEEEKQSMKKKLDKVLKNY-----DTICQINSE 3515
Cdd:pfam15921  684 RNKSEEMETTTNKLKMQlKSAQSELEQTRNTLKSMEGSdGHAMKVAMGMQKQITAKRGQIDALQSKiqfleEAMTNANKE 763

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34577049   3516 RYLQLERAQSLVnqfwetyEELWPWLTETQSIisqlpapALEYETLRQQQeehRQLRELIAEHKPHIDK 3584
Cdd:pfam15921  764 KHFLKEEKNKLS-------QELSTVATEKNKM-------AGELEVLRSQE---RRLKEKVANMEVALDK 815
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 2213-2321 2.39e-03

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: 40.76  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   2213 NNLTQFQTVEAQLKQWLVEKELMVSVlGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLrg 2292
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-- 77

                           90       100
                   ....*....|....*....|....*....
gi 34577049   2293 iVKEQLAAVTQKWDSLTGQLSDRCDWIDQ 2321
Cdd:pfam00435   78 -IQERLEELNERWEQLLELAAERKQKLEE 105
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1259-1403 2.69e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1259 MIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENfLKENGEKLSQEDKALIEQKLNEAKIKCEQlnlKAEQSKKE 1338
Cdd:PRK00409  510 LIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEK-LKEELEEKKEKLQEEEDKLLEEAEKEAQQ---AIKEAKKE 585

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34577049  1339 LDKVVTTAIKEETEKVAAVK--QLEESKTKIenlldwlsnvdKDSERAGTKHKQVIEQNGTHFQEGD 1403
Cdd:PRK00409  586 ADEIIKELRQLQKGGYASVKahELIEARKRL-----------NKANEKKEKKKKKQKEKQEELKVGD 641
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 868-1032 2.90e-03

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: 42.43  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  868 KLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEdelQKAKAISDEmfktykeRDLDFDWHKEKADQLVERWQN 947
Cdd:cd00176   21 ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN---ELGEQLIEE-------GHPDAEEIQERLEELNQRWEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  948 VHVQIDNRLRDLEGIGKSLKYYRDTYHpLDDWIQqvETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQK 1027
Cdd:cd00176   91 LRELAEERRQRLEEALDLQQFFRDADD-LEQWLE--EKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167


                 ....*
gi 34577049 1028 YAEQY 1032
Cdd:cd00176  168 LAEEL 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1153-1555 3.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1153 EEISTKKEQLSEALQTIqlflakhgdKMTDEERNELEKQVKTLQESYNLLFS-ESLKQLQESQTSGDVKVEEKIVAERQQ 1231
Cdd:PRK03918  331 KELEEKEERLEELKKKL---------KELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPEKLEKELEELEKAKE 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1232 EYKEKLQGICDLLTQTENR------------------------LIGHQEAFMIGDGTVELKKYQSKQEELQKDMQgsaqA 1287
Cdd:PRK03918  402 EIEEEISKITARIGELKKEikelkkaieelkkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKER----K 477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1288 LAEVVKNTENFLKENGEKLSQEDKAlieQKLNEAKIKCEQLNL-KAEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTK 1366
Cdd:PRK03918  478 LRKELRELEKVLKKESELIKLKELA---EQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1367 IENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKsaIGEEDEVNGNLLE-TDVDGQVGTTQENLnqqyQKVKAQH 1445
Cdd:PRK03918  555 KKKLAELEKKLDELEEELAELLKELEELGFESVEELEER--LKELEPFYNEYLElKDAEKELEREEKEL----KKLEEEL 628

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1446 EKIISQHQAVIIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEh 1525
Cdd:PRK03918  629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE- 707

                         410       420       430
                  ....*....|....*....|....*....|
gi 34577049  1526 wlqQSEQELENLEAGADDINGLMTKLKRQK 1555
Cdd:PRK03918  708 ---KAKKELEKLEKALERVEELREKVKKYK 734
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 627-1368 3.30e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 44.27  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    627 NRIEQQYQNVLTlwHESHINMKSVVSWHYLINEIDRIRASNVASIKTmlpgehqQVLSNLQSRFEDFLEDSQESQVFSGS 706
Cdd:TIGR01612 1029 NDIEQKIEDANK--NIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK-------EILEEAEINITNFNEIKEKLKHYNFD 1099

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    707 DITqleKEVNVckQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIrtplerDDLhESVFRITEQEKL 786
Cdd:TIGR01612 1100 DFG---KEENI--KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI------NDL-EDVADKAISNDD 1167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    787 KKELERLKDDLGTITNKCEEFFSqaaasssvptlrsELNVVLQNMNQVySMSSTYIDKLKTVNLvlkntQAAEALVKLYE 866
Cdd:TIGR01612 1168 PEEIEKKIENIVTKIDKKKNIYD-------------EIKKLLNEIAEI-EKDKTSLEEVKGINL-----SYGKNLGKLFL 1228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    867 TKLCEEeaviadKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEM--FKTYKERDLDFDWHKEKADQLVER 944
Cdd:TIGR01612 1229 EKIDEE------KKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMetFNISHDDDKDHHIISKKHDENISD 1302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    945 WQNvhvqidnrlrdlegigKSLKYYRDTYHPLDdwIQQVETT-QRKIQENQPENSKtLATQLNQQKMLVSEIEMKQSK-- 1021
Cdd:TIGR01612 1303 IRE----------------KSLKIIEDFSEESD--INDIKKElQKNLLDAQKHNSD-INLYLNEIANIYNILKLNKIKki 1363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1022 MDECQKYA---EQYSATVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSAD-----LIIQEFMDLRTRYTALVTLMTQYIK 1093
Cdd:TIGR01612 1364 IDEVKEYTkeiEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDdkdidECIKKIKELKNHILSEESNIDTYFK 1443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1094 ------------FAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNI--SKTLKDAEKAGKPPFSKQKISSEEIstkK 1159
Cdd:TIGR01612 1444 nadennenvlllFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIdkSKGCKDEADKNAKAIEKNKELFEQY---K 1520

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1160 EQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSgDVKVEEKiVAERQQEYKEKLqG 1239
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE-KFRIEDD-AAKNDKSNKAAI-D 1597

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1240 ICDLLTQTENRLIGHQE-AFMIGDGTVELKKYQSKQEELQKDMQGSaqALAEVVKNTeNFLKENGEKLSQEDKALIEQK- 1317
Cdd:TIGR01612 1598 IQLSLENFENKFLKISDiKKKINDCLKETESIEKKISSFSIDSQDT--ELKENGDNL-NSLQEFLESLKDQKKNIEDKKk 1674

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|..
gi 34577049   1318 -LNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEETekVAAVKQLEESKTKIE 1368
Cdd:TIGR01612 1675 eLDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIA--IANKEEIESIKELIE 1724
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1474-2022 3.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1474 SPEEKEKLQKNMKELKvHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEagaDDINGLMTKLKR 1553
Cdd:PRK03918  143 SDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL---REINEISSELPE 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1554 QKSFSEDVISHKGDLRYITisgNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLgNNLKDLVDK 1633
Cdd:PRK03918  219 LREELEKLEKEVKELEELK---EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEE 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1634 YQHYEDASCGLLAGLQACEATASKhLSEPIavdpKNLQRQLEE-------TKALQGQISSQQVAVEKLKKTAEVLLDARg 1706
Cdd:PRK03918  295 YIKLSEFYEEYLDELREIEKRLSR-LEEEI----NGIEERIKEleekeerLEELKKKLKELEKRLEELEERHELYEEAK- 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1707 SLLPAKNDIQKTLDDivgryedlsKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKE-----------QGQVP 1775
Cdd:PRK03918  369 AKKEELERLKKRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkaKGKCP 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1776 LNSTALQDIISKNIMLE-----QDIAGRQSSINAMNEKVKK-FMETTDPSTASSLQAKMKDLSARFSEASHKHKETlaKM 1849
Cdd:PRK03918  440 VCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKeLRELEKVLKKESELIKLKELAEQLKELEEKLKKY--NL 517

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1850 EELKTKVELFENLSEKLQTfLETKTQALTevdvpgKDVTELSQYmqESTSEFLEHKKHL--EVLHSLLKEISSHGLPSDK 1927
Cdd:PRK03918  518 EELEKKAEEYEKLKEKLIK-LKGEIKSLK------KELEKLEEL--KKKLAELEKKLDEleEELAELLKELEELGFESVE 588

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049  1928 AL-----VLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDT 2002
Cdd:PRK03918  589 ELeerlkELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668

                         570       580
                  ....*....|....*....|
gi 34577049  2003 KKLQEKWSLKTPEIQKVNNS 2022
Cdd:PRK03918  669 LELSRELAGLRAELEELEKR 688
SPEC smart00150
Spectrin repeats;
2217-2315 3.88e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.01  E-value: 3.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    2217 QFQTVEAQLKQWLVEKELMVSVLgPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSlrgIVKE 2296
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE---EIEE 77

                            90
                    ....*....|....*....
gi 34577049    2297 QLAAVTQKWDSLTGQLSDR 2315
Cdd:smart00150   78 RLEELNERWEELKELAEER 96
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 881-1372 4.12e-03

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: 43.57  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    881 NIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISD-EMFKTYKERD---------------LDFDWHKEKADQLVER 944
Cdd:pfam15921  318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDqfsqesgnlddqlqkLLADLHKREKELSLEK 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049    945 WQNVH---------VQIDNRLRDLEGIGKSLKYYRDTYHPLDDWIQ-QVETTQRKIQ-ENQP-ENSKTLATQLNQQKML- 1011
Cdd:pfam15921  398 EQNKRlwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQgKNESlEKVSSLTAQLESTKEMl 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1012 ---VSEIEMKQSKMDECQKYAEQYSATVKDYElqtmtyRAMvdsqQKSPVKRRRMQSSADLIIQEFmdlrtrytalvtlm 1088
Cdd:pfam15921  478 rkvVEELTAKKMTLESSERTVSDLTASLQEKE------RAI----EATNAEITKLRSRVDLKLQEL-------------- 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1089 tQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTL-KDAEKAGKPPFSKQKIsSEEISTKKEQLSE--- 1164
Cdd:pfam15921  534 -QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgQHGRTAGAMQVEKAQL-EKEINDRRLELQEfki 611

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1165 -------------------ALQTIQLFLAK----HGDKMTDEERNELEKQVKTLQESYNLLfSESLKQLQESQTSgdvKV 1221
Cdd:pfam15921  612 lkdkkdakirelearvsdlELEKVKLVNAGserlRAVKDIKQERDQLLNEVKTSRNELNSL-SEDYEVLKRNFRN---KS 687

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1222 EEkiVAERQQEYKEKLQGICDLLTQTENRLI------GHQEAFMIGdgtvELKKYQSKQEELQKdMQGSAQALAEVVKNT 1295
Cdd:pfam15921  688 EE--METTTNKLKMQLKSAQSELEQTRNTLKsmegsdGHAMKVAMG----MQKQITAKRGQIDA-LQSKIQFLEEAMTNA 760

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1296 ---ENFLKENGEKLSQEDKALIEQKLNEAK----IKCEQLNLKAEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIE 1368
Cdd:pfam15921  761 nkeKHFLKEEKNKLSQELSTVATEKNKMAGelevLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840


                   ....
gi 34577049   1369 NLLD 1372
Cdd:pfam15921  841 HTLD 844
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 4787-4904 4.33e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 42.43  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 4787 KSRVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKI 4866
Cdd:cd15899   34 KRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIK 113

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 34577049 4867 EDEVTRQVakckcakrfqveqIGDNKYRFFLGNQFGDS 4904
Cdd:cd15899  114 EDEEYKKL-------------LLKDKKRFEAADQDGDL 138
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1153-1518 4.40e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1153 EEISTKKEQLSEALQTIQLFLAKHGDKMtdEERNELEKQVKTLQEsynlLFSESLKQLQE-SQTSGDVKVEEKIVAERQQ 1231
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIE--KEIEQLEQEEEKLKE----RLEELEEDLSSlEQEIENVKSELKELEARIE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1232 EYKEKLQGICDLLTQTENRLiGHQEAFMIGDGTVELKKYQSKQEELQKDmqgsaqalAEVVKNTENFLKENGEKLSQEDK 1311
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLRE--------IEQKLNRLTLEKEYLEKEIQELQ 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1312 A-LIEQKLNEAKIKCEQLNLKAEQSKKEldkvvttaiKEETEKVAAVKQLEESKTKIEnlldwlsnvdKDSERAgTKHKQ 1390
Cdd:TIGR02169  840 EqRIDLKEQIKSIEKEIENLNGKKEELE---------EELEELEAALRDLESRLGDLK----------KERDEL-EAQLR 899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1391 VIEQNgthfqEGDGKSAIgEEDEVNGNLLETdvdgqvgtTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQG 1470
Cdd:TIGR02169  900 ELERK-----IEELEAQI-EKKRKRLSELKA--------KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34577049   1471 Q--------YLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEE-----LEKFDA 1518
Cdd:TIGR02169  966 EiralepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKkrevfMEAFEA 1026
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1185-1953 5.17e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 5.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1185 RNELEkQVKTLQESYNLLFSESLKQLQESQTSGDVKVEEKIVAERQQEYK--EKLQGICDLLTQ---TENRLIGHQEafm 1259
Cdd:TIGR02169  176 LEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgyELLKEKEALERQkeaIERQLASLEE--- 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1260 igdgtvELKKYQSKQEELQKDMQGSAQALAEVVK-------NTENFLKENGEKLSQEdKALIEQKLNEAKIKCEQLNLKA 1332
Cdd:TIGR02169  252 ------ELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeEEQLRVKEKIGELEAE-IASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1333 EQSKKELDKV------VTTAIKEETEKVAAVK-QLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQngthfqegdgK 1405
Cdd:TIGR02169  325 AKLEAEIDKLlaeieeLEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK----------L 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1406 SAIGEE-DEVNGNLletdvdGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQgqylspeeKEKLQKN 1484
Cdd:TIGR02169  395 EKLKREiNELKREL------DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------EWKLEQL 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1485 MKELKvhyetalaesekkmklthSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINglmtklKRQKSFS--EDVI 1562
Cdd:TIGR02169  461 AADLS------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE------ERVRGGRavEEVL 516

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1563 SHKGDLRYITISG-NRVLEA-AKSCSKRDGGK-----VDTSATHREV-----QRKLDHAT----------DRFRSLYSKC 1620
Cdd:TIGR02169  517 KASIQGVHGTVAQlGSVGERyATAIEVAAGNRlnnvvVEDDAVAKEAiellkRRKAGRATflplnkmrdeRRDLSILSED 596

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1621 NVLGNNLkDLVDKYQHYEDA------SCGLLAGLQACE-------------------------ATASKHLSEPIAVDPKN 1669
Cdd:TIGR02169  597 GVIGFAV-DLVEFDPKYEPAfkyvfgDTLVVEDIEAARrlmgkyrmvtlegelfeksgamtggSRAPRGGILFSRSEPAE 675

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1670 LQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARgsllpakNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSLS 1749
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-------SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1750 VQDGLDEMLDWMGNVESSLKEQgqvPLNSTALQDIISKnimLEQDIAGRQ-SSINAMNEKVKKFMETTDpSTASSLQAKM 1828
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEEL---EEDLHKLEEALND---LEARLSHSRiPEIQAELSKLEEEVSRIE-ARLREIEQKL 821

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1829 KDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDvpgKDVTELSQYMQESTSEFLEHKKHL 1908
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 34577049   1909 EVLHSLLKEISS--HGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKE 1953
Cdd:TIGR02169  899 RELERKIEELEAqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2195-2423 5.21e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2195 QELNQLtidrQQKLEESSNNLTQFQT------VEAQLKQwlVEKELmvsvlgplsidpNMLNTQRQQVQILLQEFATRKP 2268
Cdd:COG3206  182 EQLPEL----RKELEEAEAALEEFRQknglvdLSEEAKL--LLQQL------------SELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049 2269 QYEQLTAAGQGILSRPGEDPSLRGIvKEQLAAVTQKWDSLTGQLSDrcdwidqaivKSTQYQSLLRSLSDKLSDLDNKLS 2348
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQL-RAQLAELEAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQ 312

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34577049 2349 SSLAvsthpdAMNQQLETAQKMKQEIQQEKKQIKvaqalcEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAE 2423
Cdd:COG3206  313 RILA------SLEAELEALQAREASLQAQLAQLE------ARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4785-4857 5.37e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 5.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34577049 4785 HKKSRVMDFFRRIDKDQDGKITRQEFIDGilsskfptSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAY 4857
Cdd:COG5126    2 LQRRKLDRRFDLLDADGDGVLERDDFEAL--------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEAT 66
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1264-1344 6.95e-03

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 42.63  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   1264 TVELKKYQSKQEE--LQKDMQGSAQA-------------LAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQL 1328
Cdd:pfam00012  494 TIEASEGLSDDEIerMVKDAEEYAEEdkkrkerieakneAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGD 573

                           90
                   ....*....|....*..
gi 34577049   1329 NLKAEQSK-KELDKVVT 1344
Cdd:pfam00012  574 DKEEIEAKtEELAQVSQ 590
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3535-3630 8.13e-03

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: 39.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3535 EELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLY 3614
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89

                           90
                   ....*....|....*.
gi 34577049   3615 SQIKEDVKKRAVALDE 3630
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 3092-3195 9.88e-03

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: 38.84  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577049   3092 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSK 3171
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82

                           90       100
                   ....*....|....*....|....
gi 34577049   3172 LDFSQVWyIEIQEKSHSRSELLQQ 3195
Cdd:pfam00435   83 EELNERW-EQLLELAAERKQKLEE 105
 
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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