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Conserved domains on  [gi|386767917|ref|NP_001246312|]
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short stop, isoform AC [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
223-327 2.02e-65

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409038  Cd Length: 105  Bit Score: 218.03  E-value: 2.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5129-5201 3.37e-40

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


:

Pssm-ID: 128539  Cd Length: 73  Bit Score: 144.51  E-value: 3.37e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917   5129 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5201
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4187-4406 2.74e-30

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: 121.40  E-value: 2.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4187 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4266
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4267 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4346
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4347 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4406
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4074-4295 1.63e-27

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: 113.69  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4074 KAMEFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQA 4153
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNE----LGEQLIEE-GHPDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4154 ASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALnELLVWINKTDSTLDQLkPIPGDPQLLEVELAKLKVLA 4233
Cdd:cd00176    75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4234 NDIQAHQNSVDTLNDAGRQLIEtEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEAL 4295
Cdd:cd00176   153 EELEAHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
864-929 2.12e-25

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 101.96  E-value: 2.12e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917   864 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 929
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4408-4627 3.64e-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: 106.76  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4408 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4487
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4488 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4567
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4568 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4627
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3641-3851 2.30e-24

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: 104.45  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3641 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3720
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3721 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3800
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 3801 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3851
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4632-4840 2.66e-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: 101.37  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4632 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4709
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4710 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4789
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 4790 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4840
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
690-866 9.62e-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: 90.97  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  690 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 769
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  770 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 849
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 386767917  850 ETVATLQRRAQTVVPLN 866
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3098-3315 1.12e-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: 90.97  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3098 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3177
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3178 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3257
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 3258 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3315
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2666-2875 1.48e-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: 90.58  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2666 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2743
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2744 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2823
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2824 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2875
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2773-2985 1.43e-18

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: 87.89  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2773 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2852
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2853 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2932
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2933 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2985
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3318-3533 3.34e-18

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: 86.73  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3318 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3397
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3398 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3477
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3478 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3533
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1959-2168 8.33e-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: 8.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1959 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 2038
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2039 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2116
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767917 2117 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2168
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3851-4072 1.61e-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: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3851 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3930
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3931 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 4010
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4011 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4072
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3535-3742 4.19e-15

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.49  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3535 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3605
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3606 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3685
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 3686 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3742
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2448-2662 1.66e-14

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2448 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2527
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2528 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2604
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 2605 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2662
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1153-1390 2.33e-10

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: 63.62  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1153 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1232
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1233 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1312
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 1313 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1390
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
5220-5452 4.02e-10

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 67.12  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5220 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5299
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5300 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5375
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 5376 TTPRPARLSVTTTTTPGSRLNGTSTITRKTASGSASPAPTRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTT 5452
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD-ATGRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
471-689 7.13e-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: 56.30  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  471 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 543
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  544 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 623
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  624 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 689
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1047-1250 1.26e-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: 55.53  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1047 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1122
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1123 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1196
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386767917 1197 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1250
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
5054-5123 6.95e-06

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5054 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5123
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
343-552 1.84e-05

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: 49.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  343 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 422
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  423 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 502
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917  503 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 552
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1628-2186 4.09e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1628 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1693
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1694 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1767
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1768 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1845
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1846 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1901
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1902 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1960
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1961 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 2011
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2012 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2082
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2083 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2158
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 386767917  2159 INISIDERAKLSKQKAEQQLAYEGLKDQ 2186
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
PLEC smart00250
Plectin repeat;
1498-1526 1.02e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 1.02e-03
                            10        20
                    ....*....|....*....|....*....
gi 386767917   1498 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1526
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
223-327 2.02e-65

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 218.03  E-value: 2.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5129-5201 3.37e-40

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


Pssm-ID: 128539  Cd Length: 73  Bit Score: 144.51  E-value: 3.37e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917   5129 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5201
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
5131-5199 2.46e-38

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: 138.88  E-value: 2.46e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767917  5131 IHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRA 5199
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4187-4406 2.74e-30

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: 121.40  E-value: 2.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4187 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4266
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4267 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4346
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4347 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4406
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4074-4295 1.63e-27

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: 113.69  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4074 KAMEFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQA 4153
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNE----LGEQLIEE-GHPDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4154 ASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALnELLVWINKTDSTLDQLkPIPGDPQLLEVELAKLKVLA 4233
Cdd:cd00176    75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4234 NDIQAHQNSVDTLNDAGRQLIEtEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEAL 4295
Cdd:cd00176   153 EELEAHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
864-929 2.12e-25

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 101.96  E-value: 2.12e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917   864 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 929
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
223-327 3.30e-25

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 103.14  E-value: 3.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   223 SAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK--ARNDRPRERLETAFHIVEKEYGVTR- 298
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 386767917   299 LLDPEDVdtNEPDEKSLITYISSLYDVFP 327
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4408-4627 3.64e-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: 106.76  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4408 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4487
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4488 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4567
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4568 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4627
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3641-3851 2.30e-24

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: 104.45  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3641 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3720
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3721 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3800
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 3801 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3851
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4632-4840 2.66e-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: 101.37  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4632 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4709
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4710 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4789
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 4790 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4840
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
690-866 9.62e-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: 90.97  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  690 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 769
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  770 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 849
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 386767917  850 ETVATLQRRAQTVVPLN 866
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3098-3315 1.12e-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: 90.97  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3098 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3177
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3178 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3257
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 3258 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3315
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2666-2875 1.48e-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: 90.58  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2666 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2743
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2744 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2823
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2824 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2875
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
226-322 2.18e-19

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 86.22  E-value: 2.18e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    226 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKAR----NDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 386767917    302 PEDVDTNEPDEKSLITYISSL 322
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2773-2985 1.43e-18

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: 87.89  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2773 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2852
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2853 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2932
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2933 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2985
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3318-3533 3.34e-18

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: 86.73  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3318 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3397
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3398 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3477
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3478 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3533
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
204-328 3.61e-18

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 92.31  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  204 SSTQRREISDIvvGKEDNVSAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRER 282
Cdd:COG5069   108 SLISRLTIATI--NEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKA 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386767917  283 LET--AFHIVEKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVFPE 328
Cdd:COG5069   186 LNNfqAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGL 234
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1959-2168 8.33e-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: 8.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1959 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 2038
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2039 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2116
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767917 2117 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2168
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3851-4072 1.61e-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: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3851 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3930
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3931 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 4010
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4011 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4072
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3535-3742 4.19e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.49  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3535 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3605
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3606 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3685
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 3686 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3742
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4190-4292 7.58e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 7.58e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4190 QFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIetEKGSVEASTTQEK 4269
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 386767917   4270 LRKLNNEWKQLLQKASDRQHELE 4292
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2448-2662 1.66e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2448 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2527
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2528 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2604
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 2605 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2662
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4186-4293 6.25e-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: 68.11  E-value: 6.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4186 LHLGQFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEAST 4265
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 386767917  4266 TQEKLRKLNNEWKQLLQKASDRQHELEE 4293
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4632-4730 1.42e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 1.42e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4632 QFSDALGELLDWLKKAKSRLnENGPVHGDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4709
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   4710 EMQSIWEEVKSAVAKRGERLQ 4730
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4077-4182 8.58e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.58  E-value: 8.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4077 EFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQAASI 4156
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNE----LGEQLIEE-GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 386767917   4157 REPLSVVNRRWEALLRGMVERQKQLE 4182
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
691-791 1.14e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.58  E-value: 1.14e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    691 QHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHLT 770
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917    771 ALQQQWAWLLQLTLCLEVHLK 791
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1153-1390 2.33e-10

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: 63.62  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1153 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1232
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1233 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1312
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 1313 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1390
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5220-5452 4.02e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 67.12  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5220 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5299
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5300 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5375
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 5376 TTPRPARLSVTTTTTPGSRLNGTSTITRKTASGSASPAPTRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTT 5452
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD-ATGRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
SPEC smart00150
Spectrin repeats;
4411-4512 5.19e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 5.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4411 EFHDTLQAFVEWLTQAEKLLSnAEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIKNLL 4490
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 386767917   4491 VSVQHRWERVVSKAAERTRALD 4512
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
5339-5454 7.14e-10

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 61.51  E-value: 7.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  5339 SKPPSRHGSTLSLDSTDDhtPSRIPQRKPSTGSTASGTTPRPARLSVTTTTTPGSRLNGTS---TITRKTA-----SGSA 5410
Cdd:pfam09595   33 LILIGESNKEAALIITDI--IDININKQHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNNqhpSQDRSEApplepAAKT 110
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386767917  5411 SPAPTRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPT 5454
Cdd:pfam09595  111 KPSEHEPA-NPPDASNRLSPPDASTAAIREARTFRKPSTGKRNN 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2841-3366 1.07e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2841 DIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDpkLLERVK 2920
Cdd:PRK02224  191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED--LRETIA 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2921 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 3000
Cdd:PRK02224  269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3001 IDLNDLETEIEKLSPPGREI-KIVQVQIDDVGKIQTKLDRLVGRLEDAERAADvlvdagfaaDTTQTREQISTLRKTLGR 3079
Cdd:PRK02224  349 EDADDLEERAEELREEAAELeSELEEAREAVEDRREEIEELEEEIEELRERFG---------DAPVDLGNAEDFLEELRE 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3080 LDNRVRDHEDNLHSTLKALREFYDHQSQTLDD------IQDVSDEfkrmkPVGSELDQIRRQQEDFrnfrERKVEPLAIN 3153
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGS-----PHVETIEEDRERVEEL----EAELEDLEEE 490
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3154 VDKVNvagrDLVRSAGSGVSTtaiEKDLEKLNDRWNDLKERMNERDRRLDvallqsgKFQEALAGLSKWLSDTE-EMVAN 3232
Cdd:PRK02224  491 VEEVE----ERLERAEDLVEA---EDRIERLEERREDLEELIAERRETIE-------EKRERAEELRERAAELEaEAEEK 556
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3233 QKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVAnhcepgERASIEKQLNDLMKRFDALTDGAEQRELDLE 3312
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA------AIADAEDEIERLREKREALAELNDERRERLA 630
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3313 EAMEVAKRFHDKISP--LELWLDNTERSVKAMELIptdEEKIQQRIREHDRLHDEI 3366
Cdd:PRK02224  631 EKRERKRELEAEFDEarIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEI 683
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3611-4299 1.65e-09

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: 65.08  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3611 NRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADlpamepKLVRAQLQEHRSINDDISSQKGRV 3690
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ------KELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3691 RDVTAASKKV---LRESPQS-----ENTATLREKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDM 3762
Cdd:TIGR02168  312 ANLERQLEELeaqLEELESKldelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3763 EQQISRLSMPALRPD-QITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALvaDDDGAKINEILDTDNARYAALRLE 3839
Cdd:TIGR02168  392 ELQIASLNNEIERLEaRLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3840 LRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPLSAL---PQKIREQIED------ND 3896
Cdd:TIGR02168  470 LEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVLSELisvDEGYEAAIEAalggrlQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3897 ALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA---------------VRDIKAKLEKLNNLW-------N 3946
Cdd:TIGR02168  550 VVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvakdLVKFDPKLRKALSYLlggvlvvD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3947 DVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEETLscqeppAAQPQDIKKQQVALQEI 4010
Cdd:TIGR02168  630 DLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEKI------EELEEKIAELEKALAEL 703
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4011 RHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLqnllkflt 4090
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------- 770
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4091 kaEDKFAHLGAVGSDIDAVKRQIEQLKSfkdevdphmvEVEALNRGLKRQAVELTERTspEQAASIREPLSVVNRRWEAL 4170
Cdd:TIGR02168  771 --EEAEEELAEAEAEIEELEAQIEQLKE----------ELKALREALDELRAELTLLN--EEAANLRERLESLERRIAAT 836
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4171 LRGMVERQKQLEHALLHLGQFQHALNELLVWINKtdstldqlkpipgdpqlLEVELAKLKVLANDIQAHQNSV-DTLNDA 4249
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----------------LESELEALLNERASLEEALALLrSELEEL 899
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 386767917  4250 GRQLIETEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALREAH 4299
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
SPEC smart00150
Spectrin repeats;
3746-3848 4.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 4.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3746 EHFADSHQGLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3825
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 386767917   3826 LDTDNARYAALRLELRERQQALE 3848
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3211-3312 5.25e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 5.25e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3211 KFQEALAGLSKWLSDTEEMVAnQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPgERASIEKQL 3290
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 386767917   3291 NDLMKRFDALTDGAEQRELDLE 3312
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3969-4068 7.10e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 7.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3969 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 4048
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 386767917   4049 DLDNAWDNITALYAKREENL 4068
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
471-689 7.13e-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: 56.30  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  471 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 543
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  544 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 623
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  624 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 689
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1047-1250 1.26e-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: 55.53  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1047 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1122
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1123 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1196
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386767917 1197 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1250
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
690-783 2.53e-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: 51.94  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   690 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 769
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 386767917   770 TALQQQWAWLLQLT 783
Cdd:pfam00435   83 EELNERWEQLLELA 96
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4037-4371 3.63e-07

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: 57.00  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4037 EPDK-PEVKKHIEDLDNAWDNITALYAKREE---NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAH-LGAVGSDIDAVKR 4111
Cdd:TIGR02169  672 EPAElQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4112 QIEQLKSFKDEVDPHMVEVEALNRGLKRQAVELTERTSPEQAASIREPLSVVN---RRWEALLRGmVERQKQLEHALLHL 4188
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEeevSRIEARLRE-IEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4189 GQ--FQHALNELLVWINKTDSTLDQLKPIPGDPQLLEVELAKLKVLANDIQA-HQNSVDTLNDAGRQLIETEKGSVEAST 4265
Cdd:TIGR02169  831 LEkeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrLGDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4266 TQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEVQDilgwLGDVDAV-------IGASKPVGGLpetATEQLER 4338
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAElqrveeeIRALEPVNML---AIQEYEE 983
                          330       340       350
                   ....*....|....*....|....*....|...
gi 386767917  4339 FMEVYNELDENRPKVETIQAQGQEYIKRQNQMK 4371
Cdd:TIGR02169  984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
SPEC smart00150
Spectrin repeats;
3320-3420 5.18e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 5.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3320 RFHDKISPLELWLDNTERSVKAMElIPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGEKV 3399
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   3400 RGVTERYTGLVDASDNIGALL 3420
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
359-685 8.28e-07

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: 55.84  E-value: 8.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   359 REKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYFETVGEVDVEAELrpdaiekawyrmn 438
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------- 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   439 taLQDREvilQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEGRRIERLhpvdaKSIVEALETEIRHleEPIQD 518
Cdd:TIGR02169  728 --LEQEE---EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-----EEALNDLEARLSH--SRIPE 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   519 MNQ------DCHVLNEGRyphVSELHKKVNKLHQRWAQLRtnfhtnlvQKLSGLKYPVHETTVTRQTRmvvESRQIDTNP 592
Cdd:TIGR02169  796 IQAelskleEEVSRIEAR---LREIEQKLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSI---EKEIENLNG 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   593 HFRDLQEHIEWCQNKLKQLlaADYGSDLPSVKEELDRQQHEHKI-IDQFHTKIlNDERQQTKFSGDELALYQQRLNQLQK 671
Cdd:TIGR02169  862 KKEELEEELEELEAALRDL--ESRLGDLKKERDELEAQLRELERkIEELEAQI-EKKRKRLSELKAKLEALEEELSEIED 938
                          330
                   ....*....|....
gi 386767917   672 VYAELLSTSTKRLS 685
Cdd:TIGR02169  939 PKGEDEEIPEEELS 952
SPEC smart00150
Spectrin repeats;
2773-2873 8.50e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 8.50e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   2773 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2852
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   2853 DIRDRWERLNNDLIARAHEIE 2873
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4407-4511 2.19e-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: 49.24  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4407 KEATEFHDTLQAFVEWLTQAEKLLSNaEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKYfSQKQDVILI 4486
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 386767917  4487 KNLLVSVQHRWERVVSKAAERTRAL 4511
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4632-4730 2.91e-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: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4632 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSGN--NPEVGRQLD 4709
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHyaSEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 386767917  4710 EMQSIWEEVKSAVAKRGERLQ 4730
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
5054-5123 6.95e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5054 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5123
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SPEC smart00150
Spectrin repeats;
1961-2065 1.36e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   1961 QGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVE 2040
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD--AEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 386767917   2041 SNLNDVTVKFEKLYEKANKRGEFLD 2065
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
343-552 1.84e-05

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: 49.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  343 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 422
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  423 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 502
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917  503 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 552
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2907-3320 2.13e-05

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: 51.22  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2907 GGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAA 2986
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2987 TAVSQFNEQMKSLGIDLNDLETEIEKLsppgreIKIVQVQIDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaadTTQT 3066
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKEL------EARIEELEEDLHKLEEALNDLEARLSHSR--------------IPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3067 REQISTLRKTLGRLDNRVRDHEDNLHStLKALREFYDHQSQTLDDIQDVSDEFKRMkpvgseldqIRRQQEDFRNFRERK 3146
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKS---------IEKEIENLNGKKEEL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3147 VEPLAinvdKVNVAGRDLVRSAGSgvsttaIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDT 3226
Cdd:TIGR02169  867 EEELE----ELEAALRDLESRLGD------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3227 EEMVANQKPPSS---DYKVVKAQLQEqkflkkmLLDRQNSMGSLANLGKEvanhcepgERASIEKQLNDLMKRFDALTdg 3303
Cdd:TIGR02169  937 EDPKGEDEEIPEeelSLEDVQAELQR-------VEEEIRALEPVNMLAIQ--------EYEEVLKRLDELKEKRAKLE-- 999
                          410
                   ....*....|....*...
gi 386767917  3304 AEQREL-DLEEAMEVAKR 3320
Cdd:TIGR02169 1000 EERKAIlERIEEYEKKKR 1017
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3641-3740 2.22e-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: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3641 DIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPQSenTATLREKLDDL 3720
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 386767917  3721 KEIVDTVAQLCSERLGILEQ 3740
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2452-2552 2.60e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 2.60e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   2452 FLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAVEIKL 2531
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   2532 KDILGKWDDLVGKLDDRANSL 2552
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1628-2186 4.09e-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: 50.44  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1628 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1693
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1694 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1767
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1768 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1845
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1846 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1901
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1902 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1960
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1961 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 2011
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2012 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2082
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2083 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2158
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 386767917  2159 INISIDERAKLSKQKAEQQLAYEGLKDQ 2186
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
EF-hand_7 pfam13499
EF-hand domain pair;
5052-5116 4.53e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 4.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917  5052 KSRLTDLFRKMDKDNNGMIPRDVFIDGI--LNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5116
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
5054-5116 6.12e-05

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: 43.69  E-value: 6.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917 5054 RLTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5116
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3211-3313 6.41e-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: 45.00  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3211 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcEPGERASIEKQL 3290
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 386767917  3291 NDLMKRFDALTDGAEQRELDLEE 3313
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
594-688 1.44e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    594 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 670
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVeaLNELGEQLIEEGHPDAEEiEERLEELN 83
                            90
                    ....*....|....*...
gi 386767917    671 KVYAELLSTSTKRLSDLD 688
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3537-3628 1.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3537 QQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIESIV 3607
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAsedlGKDLESVEALlkkheAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   3608 TRDNRRFDSIVEQIQRKAERL 3628
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1712-1957 2.07e-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: 45.90  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1712 ELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKFVDESKEflailnd 1791
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1792 frtslperlphveplssAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDkANEWLRSvhpRVSRIIS 1871
Cdd:cd00176    73 -----------------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEE---KEAALAS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1872 EPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSlggqLSPMEINQLELPIADLKNNYQQLLDNLGEHCK 1951
Cdd:cd00176   132 EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQK 207

                  ....*.
gi 386767917 1952 TLDKTL 1957
Cdd:cd00176   208 KLEEAL 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2843-3100 2.39e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2843 DKEPIKAELQDIRDRWERLNndliaRAHE-IENCSRRLDDFnDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKA 2921
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLE-----RAHEaLEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2922 IREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGL-ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 3000
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3001 IDLNDLETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLVDAgFAADTTQTREQISTLRKTLGRL 3080
Cdd:COG4913   373 LPLPASAEEFAAL--------------------RAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASL 431
                         250       260
                  ....*....|....*....|
gi 386767917 3081 DNRVRDHEDNLHSTLKALRE 3100
Cdd:COG4913   432 ERRKSNIPARLLALRDALAE 451
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
885-922 2.44e-04

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386767917  885 KQQGQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIP 922
Cdd:cd11768    11 IEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIP 48
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
376-567 3.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  376 EMKRLLSDLQRFRSDEVSARKREK------------SKLIQIYKELERYFETVGEVDVEaELRPDA--IEKAWYRMNTaL 441
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLE-ELEKKAeeYEKLKEKLIK-L 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  442 QDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEG--------RRIERLHP--------VDAKSIVEAL 505
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleERLKELEPfyneylelKDAEKELERE 617
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917  506 ETEIRHLEEPIQDMNQDCHVLNEgrypHVSELHKKVNKLHQRWAQLR----TNFHTNLVQKLSGLK 567
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEK----RLEELRKELEELEKKYSEEEyeelREEYLELSRELAGLR 679
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4102-4182 4.06e-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: 42.69  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4102 VGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQAASIREPLSVVNRRWEALLRGMVERQKQL 4181
Cdd:pfam00435   29 YGKDLESVQALLKKHKALEAELAAHQDRVEALNE----LAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKL 103

                   .
gi 386767917  4182 E 4182
Cdd:pfam00435  104 E 104
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1999-2181 4.37e-04

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 46.71  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1999 IREHKVLLADLQSHQASIDSVQVSAKHLLASASNARI--AKKVESNLNDVtvkfekLYEKANKRGEFLDDVYNRLSRYLD 2076
Cdd:COG5391   303 FSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGvfAKRLEQNQNSI------LNEGVVQAETLRSSLKELLTQLQD 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2077 EISTVEQRMASLQEALDSRETSLLSTEELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQW 2156
Cdd:COG5391   377 EIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDK 456
                         170       180       190
                  ....*....|....*....|....*....|
gi 386767917 2157 RNI----NISIDERAKLSKQ-KAEQQLAYE 2181
Cdd:COG5391   457 EKLeeqlAIAEKDAQEINEElKNELKFFFS 486
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
878-926 4.62e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 40.98  E-value: 4.62e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 386767917    878 VQAICAYKQQ--GQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACL 926
Cdd:smart00326    5 VRALYDYTAQdpDELSFKKGDIITVLEKSDDGWWKGRLGRGKEGLFPSNYV 55
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1566-2078 9.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 9.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1566 RELSLLEVIQREISEAESGYETAEKRIKqAVFEKFNMCEENVNDLLKWVTTVEQKIssvGGPREKIDELRNQINALKQIK 1645
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1646 DEIESQqRPVATCLEQIRQIVLTGGDVLSAPEVT--TLENSGRELRSRVDRVNDRTVRLlRRLEAGRDELTKLRSELDVF 1723
Cdd:PRK03918  283 KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRlsRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1724 SDWLQVARRTLEDKERSLSDLTRLPSQaDSVREfvsdvighqadLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHV 1803
Cdd:PRK03918  361 HELYEEAKAKKEELERLKKRLTGLTPE-KLEKE-----------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1804 EPLSSAES-------PIRQE-----VSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDKAN---------EWLRSV 1862
Cdd:PRK03918  429 EELKKAKGkcpvcgrELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKEL 508
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1863 HPRVSRIISEP-----------------IAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSLGgQLSPMEI 1925
Cdd:PRK03918  509 EEKLKKYNLEElekkaeeyeklkeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1926 NQLELPIADLKNNY-------------QQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIK 1992
Cdd:PRK03918  588 EELEERLKELEPFYneylelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELR 665
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1993 ERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANK-RGEFLDDVYNRL 2071
Cdd:PRK03918  666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKyKALLKERALSKV 745

                  ....*..
gi 386767917 2072 SRYLDEI 2078
Cdd:PRK03918  746 GEIASEI 752
PLEC smart00250
Plectin repeat;
1498-1526 1.02e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 1.02e-03
                            10        20
                    ....*....|....*....|....*....
gi 386767917   1498 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1526
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1153-1253 1.38e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.16  E-value: 1.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   1153 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1232
Cdd:smart00150    7 ADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   1233 RLNTRWSAVCNQLGERMRSCE 1253
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3674-3942 1.41e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3674 QEHRSINDDISSQKGRVRDVTAASKKVLRESPQSENTATLREKLDDLKEIVDTVAQLcSERLGILEQALPLSEHFADSHQ 3753
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3754 GLTAWLDDMEQQISRLSmpalrpDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEAlgALVADDDGAKINEILDtdnARY 3833
Cdd:COG4913   696 ELEAELEELEEELDELK------GEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGD---AVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3834 AALRLELRERQQALESALQESSQfsdKLEGMLRALANT-VDQVNQLDP-LSALP--QKIREQIEDndalmDDL-DKRQDA 3908
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEE---ELERAMRAFNREwPAETADLDAdLESLPeyLALLDRLEE-----DGLpEYEERF 836
                         250       260       270
                  ....*....|....*....|....*....|....
gi 386767917 3909 FSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLN 3942
Cdd:COG4913   837 KELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
986-1169 1.68e-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: 45.06  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   986 EQRTAIRRALNDDA--DKLLSEGDPNDPQLRRLRRE----MDEVNRLFDEFEK-RARAEEESKQASRIFtEECLAIKSKL 1058
Cdd:TIGR02169  316 ELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDlRAELEEVDKEFAETR-DELKDYREKL 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1059 EDMARELDQIIlAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALKtpvLKKSLDNLMELWKELNTQsgl 1138
Cdd:TIGR02169  395 EKLKREINELK-RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSKY--- 467
                          170       180       190
                   ....*....|....*....|....*....|.
gi 386767917  1139 hKDRLKLLEASLAGLEDNehvISELENELAR 1169
Cdd:TIGR02169  468 -EQELYDLKEEYDRVEKE---LSKLQRELAE 494
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3320-3414 1.70e-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: 41.15  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3320 RFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKV 3399
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERL 82
                           90
                   ....*....|....*
gi 386767917  3400 RGVTERYTGLVDASD 3414
Cdd:pfam00435   83 EELNERWEQLLELAA 97
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
4214-4434 3.36e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4214 PIPGDPQL--LEVELAKLKVLANDIQAHQNSVDT-LNDAGRQLIETEKgsvEASTTQEKLRKLNNEWKQLLQKASDRQHE 4290
Cdd:COG3883    11 PAFADPQIqaKQKELSELQAELEAAQAELDALQAeLEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4291 LEEALREAhgYIAEvqdilGWLGDVDAVIGAskpvgglpETATEQLERFMevyneldenrpKVETIQAQGQEYIKRQNQM 4370
Cdd:COG3883    88 LGERARAL--YRSG-----GSVSYLDVLLGS--------ESFSDFLDRLS-----------ALSKIADADADLLEELKAD 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767917 4371 KVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDTLQAFVEWLTQAEKLLSNAE 4434
Cdd:COG3883   142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1571-1769 4.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1571 LEVIQREISEAESGYETAEKRIKQAVfEKFNMCEENVNDLLKWVTTVEQKISSVggpREKIDELRNQINALKQikdEIES 1650
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALL-KQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRA---ELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1651 QQRPVAtclEQIRQIVLTGGD-----VLSAPEVTTLENSGRELRSRVDRVNDRTVRL---LRRLEAGRDELTKLRSELDV 1722
Cdd:COG4942   102 QKEELA---ELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELEA 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386767917 1723 FSDWLQVARRTLE-DKERSLSDLTRLPSQADSVREFVSDVIGHQADLR 1769
Cdd:COG4942   179 LLAELEEERAALEaLKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1964-2066 5.72e-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: 39.61  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1964 QDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVESNL 2043
Cdd:pfam00435    8 RDADD-LESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 386767917  2044 NDVTVKFEKLYEKANKRGEFLDD 2066
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2801-3133 5.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2801 SKAKLETRLRDLQTFRSEVWKHSGEFENT-------KGLGETFLSSCDIdKEPIKAELQDIR---DRWERLNNDLIARAH 2870
Cdd:PRK03918  253 SKRKLEEKIRELEERIEELKKEIEELEEKvkelkelKEKAEEYIKLSEF-YEEYLDELREIEkrlSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2871 EIENCSRRLDDFNDELRNLDHSLGRCEdrlaahdalggaaKDPKLLERVKAIREELTNLSKPLQSLKAlaKDISAEARAA 2950
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELE-------------ERHELYEEAKAKKEELERLKKRLTGLTP--EKLEKELEEL 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2951 GGDADHLTSEVDGLADRMSELQGRLDDR---CGELQSAATAVSQFN---------EQMKSLGIDLNDLETEIEKLSPPGR 3018
Cdd:PRK03918  397 EKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGrelteehrkELLEEYTAELKRIEKELKEIEEKER 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3019 EIKIVQVQIDDVGKIQTKLDRL---------------VGRLEDAERAA----------------------DVLVDAGFAA 3061
Cdd:PRK03918  477 KLRKELRELEKVLKKESELIKLkelaeqlkeleeklkKYNLEELEKKAeeyeklkekliklkgeikslkkELEKLEELKK 556
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3062 DTTQTREQISTLRKTLGRLDNRVRD----HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIR 3133
Cdd:PRK03918  557 KLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1994-2187 9.38e-03

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: 42.74  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1994 RLQEQIREHK--VLLADLQSHQASIDSVQVSAKhllasaSNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRL 2071
Cdd:TIGR02168  217 ELKAELRELElaLLVLRLEELREELEELQEELK------EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2072 SRYLDEISTVEQRMASLQEALDSRETSLLSTE-----------ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDvt 2140
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEaqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELE-- 368
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 386767917  2141 dtgVLRDRIKALESQWRNINisiDERAKLSKQKAEQQLAYEGLKDQV 2187
Cdd:TIGR02168  369 ---ELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARL 409
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
223-327 2.02e-65

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 218.03  E-value: 2.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
223-326 9.63e-44

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 156.03  E-value: 9.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21194    82 EDVDVARPDEKSIMTYVASYYHYF 105
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
223-326 9.10e-41

second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409097  Cd Length: 105  Bit Score: 147.54  E-value: 9.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21248     2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21248    82 EDVNVEQPDEKSIITYVVTYYHYF 105
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5129-5201 3.37e-40

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


Pssm-ID: 128539  Cd Length: 73  Bit Score: 144.51  E-value: 3.37e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917   5129 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5201
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
223-326 4.99e-40

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 145.53  E-value: 4.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21319    85 EDVFTENPDEKSIITYVVAFYHYF 108
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
211-326 5.03e-40

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 145.58  E-value: 5.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  211 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 290
Cdd:cd21216     1 IQDISV---EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386767917  291 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21216    78 EKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
223-327 2.04e-39

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 143.61  E-value: 2.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21243     5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21243    85 EDVDVDKPDEKSIMTYVAQFLKKYP 109
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
5131-5199 2.46e-38

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: 138.88  E-value: 2.46e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767917  5131 IHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRA 5199
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
223-327 2.72e-38

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409088  Cd Length: 104  Bit Score: 140.51  E-value: 2.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 302
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21239    80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
221-327 7.73e-37

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409089  Cd Length: 107  Bit Score: 136.33  E-value: 7.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  221 NVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLL 300
Cdd:cd21240     2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                          90       100
                  ....*....|....*....|....*..
gi 386767917  301 DPEDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21240    81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
223-326 1.40e-36

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 135.76  E-value: 1.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21249     4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21249    84 EDVAVPHPDERSIMTYVSLYYHYF 107
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
223-326 3.22e-36

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409170  Cd Length: 119  Bit Score: 135.18  E-value: 3.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21321    85 EDVNVDQPDEKSIITYVATYYHYF 108
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
223-327 6.18e-36

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 133.70  E-value: 6.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21192     3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEV 82
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21192    83 EDVLVDKPDERSIMTYVSQFLRMFP 107
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
222-327 6.31e-36

second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409087  Cd Length: 106  Bit Score: 133.61  E-value: 6.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  222 VSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21238     1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                          90       100
                  ....*....|....*....|....*.
gi 386767917  302 PEDVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
228-327 8.83e-35

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409036  Cd Length: 104  Bit Score: 130.24  E-value: 8.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  228 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDT 307
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
                          90       100
                  ....*....|....*....|
gi 386767917  308 NEPDEKSLITYISSLYDVFP 327
Cdd:cd21187    85 EQPDKKSILMYVTSLFQVLP 104
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
228-332 1.02e-33

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 127.74  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  228 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK-ARNDRPRERLETAFHIVEKEYGVTRLLDPEDVD 306
Cdd:cd21233     5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
                          90       100
                  ....*....|....*....|....*.
gi 386767917  307 TNEPDEKSLITYISSLYDVFPEPPSI 332
Cdd:cd21233    85 TAHPDKKSILMYVTSLFQVLPQQVSI 110
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
210-326 2.55e-33

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409171  Cd Length: 130  Bit Score: 127.09  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  210 EISDIVVGKEDNV---SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETA 286
Cdd:cd21322     1 QIQVIKIETEDNRetrSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386767917  287 FHIVEKEYGVTRLLDPEDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21322    81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYF 120
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
211-326 1.09e-32

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 124.56  E-value: 1.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  211 ISDIvvgKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 290
Cdd:cd21291     1 IADI---NEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386767917  291 EKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVF 326
Cdd:cd21291    78 SKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
228-327 6.14e-32

second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 122.37  E-value: 6.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  228 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDT 307
Cdd:cd21234     5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
                          90       100
                  ....*....|....*....|
gi 386767917  308 NEPDEKSLITYISSLYDVFP 327
Cdd:cd21234    85 QLPDKKSIIMYLTSLFEVLP 104
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
223-326 8.20e-32

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 122.13  E-value: 8.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21320    82 EDISVDHPDEKSIITYVVTYYHYF 105
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
222-320 1.41e-30

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 118.40  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  222 VSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21244     4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                          90
                  ....*....|....*....
gi 386767917  302 PEDVDTNEPDEKSLITYIS 320
Cdd:cd21244    84 PEDVDVVNPDEKSIMTYVA 102
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4187-4406 2.74e-30

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: 121.40  E-value: 2.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4187 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4266
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4267 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4346
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4347 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4406
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
224-327 3.14e-30

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409094  Cd Length: 106  Bit Score: 117.20  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  224 AREALLRWARRSTARYpGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 303
Cdd:cd21245     4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
                          90       100
                  ....*....|....*....|....
gi 386767917  304 DVDTNEPDEKSLITYISSLYDVFP 327
Cdd:cd21245    83 DVMVDSPDEQSIMTYVAQFLEHFP 106
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
226-326 3.85e-30

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 117.00  E-value: 3.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  226 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPED- 304
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                          90       100
                  ....*....|....*....|..
gi 386767917  305 VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd22198    83 ASLAVPDKLSMVSYLSQFYEAF 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
223-326 2.95e-29

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 114.75  E-value: 2.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21253     1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21253    81 EDmVALKVPDKLSILTYVSQYYNYF 105
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
211-326 1.18e-28

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409136  Cd Length: 124  Bit Score: 113.64  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  211 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 290
Cdd:cd21287     1 IQDISV---EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386767917  291 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21287    78 EKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
224-326 1.97e-28

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 112.25  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  224 AREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 303
Cdd:cd21197     1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                          90       100
                  ....*....|....*....|....
gi 386767917  304 D-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21197    81 DmVTMHVPDRLSIITYVSQYYNHF 104
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
211-326 3.15e-28

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 112.51  E-value: 3.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  211 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 290
Cdd:cd21289     1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386767917  291 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21289    78 EKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
208-326 3.47e-28

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 112.49  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  208 RREISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAF 287
Cdd:cd21290     1 RFAIQDISV---EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386767917  288 HIVEKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21290    78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4074-4295 1.63e-27

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: 113.69  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4074 KAMEFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQA 4153
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNE----LGEQLIEE-GHPDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4154 ASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALnELLVWINKTDSTLDQLkPIPGDPQLLEVELAKLKVLA 4233
Cdd:cd00176    75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4234 NDIQAHQNSVDTLNDAGRQLIEtEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEAL 4295
Cdd:cd00176   153 EELEAHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
224-329 1.72e-26

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 106.88  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  224 AREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 303
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                          90       100
                  ....*....|....*....|....*..
gi 386767917  304 D-VDTNEPDEKSLITYISSLYDVFPEP 329
Cdd:cd21252    81 DmVSMKVPDCLSIMTYVSQYYNHFSNP 107
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
864-929 2.12e-25

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 101.96  E-value: 2.12e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917   864 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 929
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
226-326 2.27e-25

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 103.31  E-value: 2.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  226 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDV 305
Cdd:cd21226     3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                          90       100
                  ....*....|....*....|.
gi 386767917  306 DTNEPDEKSLITYISSLYDVF 326
Cdd:cd21226    83 MTGNPDERSIVLYTSLFYHAF 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
223-327 3.30e-25

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 103.14  E-value: 3.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   223 SAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK--ARNDRPRERLETAFHIVEKEYGVTR- 298
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 386767917   299 LLDPEDVdtNEPDEKSLITYISSLYDVFP 327
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4408-4627 3.64e-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: 106.76  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4408 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4487
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4488 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4567
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4568 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4627
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
211-326 4.67e-25

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


Pssm-ID: 409137  Cd Length: 124  Bit Score: 103.23  E-value: 4.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  211 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 290
Cdd:cd21288     1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386767917  291 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21288    78 EKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
223-326 2.06e-24

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 100.58  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 302
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21198    80 ADmVLLSVPDKLSVMTYLHQIRAHF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3641-3851 2.30e-24

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: 104.45  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3641 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3720
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3721 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3800
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 3801 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3851
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4632-4840 2.66e-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: 101.37  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4632 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4709
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4710 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4789
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917 4790 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4840
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
223-323 3.96e-23

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 97.03  E-value: 3.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|...
gi 386767917  303 ED--VDTNEPDEKSLITYISSLY 323
Cdd:cd21200    81 EDmvRMGNRPDWKCVFTYVQSLY 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3969-4185 1.36e-22

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: 99.44  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3969 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 4048
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4049 DLDNAWDNITALYAKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLgAVGSDIDAVKRQIEQLKSFKDEVDPHMV 4128
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 4129 EVEALNrglkRQAVELTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHAL 4185
Cdd:cd00176   161 RLKSLN----ELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3746-3963 4.05e-22

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: 97.90  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3746 EHFADSHQGLTAWLDDMEQQISRLSMPAlRPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3825
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3826 LDTDNARYAALRLELRERQQALESALQESSQFSDKLEgMLRALANTVDQVNQLDPLSALpQKIREQIEDNDALMDDLDKR 3905
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 3906 QDAFSAVQRAANDVIAKAGNKADPAvrdIKAKLEKLNNLWNDVQNATKKRGSSLDDIL 3963
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDADEE---IEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
223-326 5.35e-22

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 93.70  E-value: 5.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYGVTRLLDP 302
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21255    80 ADmVLLPIPDKLIVMTYLCQLRAHF 104
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
228-326 3.24e-21

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 92.03  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  228 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD-PEDVD 306
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|
gi 386767917  307 TNEPDEKSLITYISSLYDVF 326
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELF 108
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
220-328 3.42e-21

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 91.93  E-value: 3.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  220 DNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRL 299
Cdd:cd21251     2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 386767917  300 LDPEDVDT-NEPDEKSLITYISSLYDVFPE 328
Cdd:cd21251    82 MTGKEMASvGEPDKLSMVMYLTQFYEMFKD 111
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
223-326 6.07e-21

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 91.27  E-value: 6.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 302
Cdd:cd21199     8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTI 86
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21199    87 DEmVSMERPDWQSVMSYVTAIYKHF 111
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
223-321 1.13e-20

second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409033  Cd Length: 103  Bit Score: 89.99  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTaryPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21184     1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
                          90       100
                  ....*....|....*....|
gi 386767917  302 PEDVDTNEPDEKSLITYISS 321
Cdd:cd21184    78 PEDMVSPNVDELSVMTYLSY 97
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
690-866 9.62e-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: 90.97  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  690 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 769
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  770 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 849
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 386767917  850 ETVATLQRRAQTVVPLN 866
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3098-3315 1.12e-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: 90.97  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3098 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3177
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3178 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3257
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 3258 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3315
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2666-2875 1.48e-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: 90.58  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2666 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2743
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2744 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2823
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2824 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2875
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4297-4512 2.05e-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: 90.20  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4297 EAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIkrqNQMKVSSSN 4376
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4377 LQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDTLQaFVEWLTQAEKLLsNAEPVSRVLETIQAQMEEHKVLQKD 4456
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 4457 VSTHREAMLLLDKKGTHLKYFSQKQDVILIKNLLVSVQHRWERVVSKAAERTRALD 4512
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
226-322 2.18e-19

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 86.22  E-value: 2.18e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    226 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKAR----NDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 386767917    302 PEDVDTNEPDEKSLITYISSL 322
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
223-323 4.28e-19

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 85.81  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|..
gi 386767917  303 ED-VDTNEPDEKSLITYISSLY 323
Cdd:cd21259    81 EDmVRMREPDWKCVYTYIQEFY 102
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4735-4907 5.70e-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: 5.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4735 DAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIK 4814
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4815 NWLSIIQQRWEEVRQWAINRESKLEQHLQSLKDLDDtIEELLAWLSGLEGTLLNlkhEQLPDEIPPVEKLIEDHKEFMEN 4894
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS---EDLGKDLESVEELLKKHKELEEE 154
                         170
                  ....*....|...
gi 386767917 4895 TARRQNEVDRACK 4907
Cdd:cd00176   155 LEAHEPRLKSLNE 167
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
228-326 6.05e-19

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 85.32  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  228 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD-PEDVD 306
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|
gi 386767917  307 TNEPDEKSLITYISSLYDVF 326
Cdd:cd21250    89 AEEPDKLSMVMYLSKFYELF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2773-2985 1.43e-18

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: 87.89  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2773 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2852
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2853 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2932
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2933 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2985
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3318-3533 3.34e-18

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: 86.73  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3318 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3397
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3398 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3477
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3478 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3533
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
204-328 3.61e-18

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 92.31  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  204 SSTQRREISDIvvGKEDNVSAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRER 282
Cdd:COG5069   108 SLISRLTIATI--NEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKA 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386767917  283 LET--AFHIVEKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVFPE 328
Cdd:COG5069   186 LNNfqAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGL 234
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3211-3424 5.13e-18

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: 85.96  E-value: 5.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3211 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCePGERASIEKQL 3290
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3291 NDLMKRFDALTDGAEQRELDLEEAMEVAKRFHDKISpLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKK 3370
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386767917 3371 PDFSDLADVTAQLMHLVSDEEAVNLGEKVRGVTERYTGLVDASDNIGALLAESR 3424
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
223-326 8.27e-18

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 81.82  E-value: 8.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 302
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21254    80 SDmVLLAVPDKLTVMTYLYQIRAHF 104
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
223-326 3.56e-17

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 80.09  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21196     3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                          90       100
                  ....*....|....*....|....
gi 386767917  303 EDVDTNEpDEKSLITYISSLYDVF 326
Cdd:cd21196    83 QAVVAGS-DPLGLIAYLSHFHSAF 105
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
223-324 7.15e-17

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 79.24  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90       100
                  ....*....|....*....|....
gi 386767917  303 ED--VDTNEPDEKSLITYISSLYD 324
Cdd:cd21261    81 EDmmVMGRKPDPMCVFTYVQSLYN 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1959-2168 8.33e-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: 8.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1959 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 2038
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2039 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2116
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767917 2117 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2168
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
223-324 8.68e-17

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409107  Cd Length: 111  Bit Score: 79.32  E-value: 8.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 302
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90       100
                  ....*....|....*....|....
gi 386767917  303 ED--VDTNEPDEKSLITYISSLYD 324
Cdd:cd21258    81 EDmmIMGKKPDSKCVFTYVQSLYN 104
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
216-326 9.38e-17

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 79.35  E-value: 9.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  216 VGKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYG 295
Cdd:cd21256     7 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVG 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 386767917  296 VTRLLDPED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21256    86 IKSTLDINEmVRTERPDWQSVMTYVTAIYKYF 117
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
225-323 1.57e-16

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 78.59  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  225 REALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPED 304
Cdd:cd21260     3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                          90       100
                  ....*....|....*....|
gi 386767917  305 -VDTNEPDEKSLITYISSLY 323
Cdd:cd21260    83 mVRMSVPDSKCVYTYIQELY 102
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3851-4072 1.61e-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: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3851 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3930
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3931 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 4010
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 4011 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4072
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
223-326 1.34e-15

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 75.84  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYGVTRLLDP 302
Cdd:cd21257     8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                          90       100
                  ....*....|....*....|....*
gi 386767917  303 ED-VDTNEPDEKSLITYISSLYDVF 326
Cdd:cd21257    87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4517-4733 1.54e-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: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4517 EAREFNDAWSGMMQYLQETEQVLdqiiEEATASKEPQKIKKYIGKLKETHRQLGAKQSVYDGTMRTGKNLLERAPkGDRP 4596
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL----SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4597 VLDKMLIELKEQWTRVWSKSIDRQRKLEEALLLSGQFSDALgELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQ 4676
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4677 DLQKRAAQMQGVLKTGRDLERSGNN---PEVGRQLDEMQSIWEEVKSAVAKRGERLQVAL 4733
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPdadEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3535-3742 4.19e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.49  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3535 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3605
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3606 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3685
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 3686 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3742
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4190-4292 7.58e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 7.58e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4190 QFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIetEKGSVEASTTQEK 4269
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 386767917   4270 LRKLNNEWKQLLQKASDRQHELE 4292
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2878-3095 8.00e-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: 76.72  E-value: 8.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2878 RLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAaggDADHL 2957
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP---DAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2958 TSEVDGLADRMSELQGRLDDRCGELQSAAtAVSQFNEQMKSLGIDLNDLETEIEKlSPPGREIKIVQVQIDDVGKIQTKL 3037
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 3038 DRLVGRLEDAERAADVLVDAGFAADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTL 3095
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2448-2662 1.66e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2448 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2527
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2528 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2604
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 2605 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2662
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
594-783 3.06e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.17  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  594 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 670
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVeaLNELGEQLIEEGHPDAEEiQERLEELN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  671 KVYAELLSTSTKRLSDLD---SLQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATI 747
Cdd:cd00176    86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 386767917  748 LDRGEALLNQQHPAS-KCIEAHLTALQQQWAWLLQLT 783
Cdd:cd00176   166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
223-328 4.78e-14

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409079  Cd Length: 103  Bit Score: 71.26  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21230     1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90       100
                  ....*....|....*....|....*..
gi 386767917  302 PEDVDTNEPDEKSLITYISSlydvFPE 328
Cdd:cd21230    78 PEEIINPNVDEMSVMTYLSQ----FPK 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4186-4293 6.25e-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: 68.11  E-value: 6.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4186 LHLGQFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEAST 4265
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 386767917  4266 TQEKLRKLNNEWKQLLQKASDRQHELEE 4293
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4632-4730 1.42e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 1.42e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4632 QFSDALGELLDWLKKAKSRLnENGPVHGDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4709
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   4710 EMQSIWEEVKSAVAKRGERLQ 4730
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
225-324 3.23e-12

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 65.82  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  225 REALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARN---DRPRERLETAFHIVEKE-YGVTRLL 300
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkspFKKRENINLFLNACKKLgLPELDLF 80
                          90       100
                  ....*....|....*....|....
gi 386767917  301 DPEDVdTNEPDEKSLITYISSLYD 324
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
222-320 4.34e-12

second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409078  Cd Length: 105  Bit Score: 65.49  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  222 VSAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLL 300
Cdd:cd21229     2 IPPKKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVL 78
                          90       100
                  ....*....|....*....|
gi 386767917  301 DPEDVDTNEPDEKSLITYIS 320
Cdd:cd21229    79 SPEDLSSPHLDELSGMTYLS 98
SPEC smart00150
Spectrin repeats;
4077-4182 8.58e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.58  E-value: 8.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4077 EFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQAASI 4156
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNE----LGEQLIEE-GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 386767917   4157 REPLSVVNRRWEALLRGMVERQKQLE 4182
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
691-791 1.14e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.58  E-value: 1.14e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    691 QHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHLT 770
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917    771 ALQQQWAWLLQLTLCLEVHLK 791
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1844-2068 1.90e-10

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: 64.00  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1844 RQREYQDALDKANEWLRSVHPRVSriiSEPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLrslggQLSPM 1923
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS---STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-----EEGHP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1924 EINQLELPIADLKNNYQQLLDNLGEHCKTLDKTLVQSQGVQDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHK 2003
Cdd:cd00176    73 DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDL--ESVEELLKKHK 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767917 2004 VLLADLQSHQASIDSVQVSAKHLLASASNARiAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVY 2068
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDA-DEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1153-1390 2.33e-10

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: 63.62  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1153 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1232
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1233 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1312
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917 1313 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1390
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4299-4403 2.79e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 2.79e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4299 HGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIKRQNQmkvSSSNLQ 4378
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP---DAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 386767917   4379 HTLRTLKQRWDAVVSRASDKKIKLE 4403
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5220-5452 4.02e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 67.12  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5220 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5299
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5300 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5375
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917 5376 TTPRPARLSVTTTTTPGSRLNGTSTITRKTASGSASPAPTRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTT 5452
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD-ATGRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
SPEC smart00150
Spectrin repeats;
4411-4512 5.19e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 5.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4411 EFHDTLQAFVEWLTQAEKLLSnAEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIKNLL 4490
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 386767917   4491 VSVQHRWERVVSKAAERTRALD 4512
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
5339-5454 7.14e-10

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 61.51  E-value: 7.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  5339 SKPPSRHGSTLSLDSTDDhtPSRIPQRKPSTGSTASGTTPRPARLSVTTTTTPGSRLNGTS---TITRKTA-----SGSA 5410
Cdd:pfam09595   33 LILIGESNKEAALIITDI--IDININKQHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNNqhpSQDRSEApplepAAKT 110
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386767917  5411 SPAPTRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPT 5454
Cdd:pfam09595  111 KPSEHEPA-NPPDASNRLSPPDASTAAIREARTFRKPSTGKRNN 153
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2560-2768 8.57e-10

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: 62.08  E-value: 8.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2560 KEFDAAVNRLREALQNISDnLDTLPTDGDHQENLRKIENLERQLEGQRPLLADVEQSAATLCNilGDPASRADVNSRVAA 2639
Cdd:cd00176     7 RDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2640 LEKQYLALQKKLDTKKAETEASLRDGRHFAEnCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHE 2719
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767917 2720 VIMLINKGKDLTDRQQDRG---VKRDLDRIQQQWEKLRREAVDRHTRLQTCM 2768
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAdeeIEEKLEELNERWEELLELAEERQKKLEEAL 213
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2841-3366 1.07e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2841 DIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDpkLLERVK 2920
Cdd:PRK02224  191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED--LRETIA 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2921 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 3000
Cdd:PRK02224  269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3001 IDLNDLETEIEKLSPPGREI-KIVQVQIDDVGKIQTKLDRLVGRLEDAERAADvlvdagfaaDTTQTREQISTLRKTLGR 3079
Cdd:PRK02224  349 EDADDLEERAEELREEAAELeSELEEAREAVEDRREEIEELEEEIEELRERFG---------DAPVDLGNAEDFLEELRE 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3080 LDNRVRDHEDNLHSTLKALREFYDHQSQTLDD------IQDVSDEfkrmkPVGSELDQIRRQQEDFrnfrERKVEPLAIN 3153
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGS-----PHVETIEEDRERVEEL----EAELEDLEEE 490
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3154 VDKVNvagrDLVRSAGSGVSTtaiEKDLEKLNDRWNDLKERMNERDRRLDvallqsgKFQEALAGLSKWLSDTE-EMVAN 3232
Cdd:PRK02224  491 VEEVE----ERLERAEDLVEA---EDRIERLEERREDLEELIAERRETIE-------EKRERAEELRERAAELEaEAEEK 556
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3233 QKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVAnhcepgERASIEKQLNDLMKRFDALTDGAEQRELDLE 3312
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA------AIADAEDEIERLREKREALAELNDERRERLA 630
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3313 EAMEVAKRFHDKISP--LELWLDNTERSVKAMELIptdEEKIQQRIREHDRLHDEI 3366
Cdd:PRK02224  631 EKRERKRELEAEFDEarIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEI 683
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3611-4299 1.65e-09

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: 65.08  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3611 NRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADlpamepKLVRAQLQEHRSINDDISSQKGRV 3690
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ------KELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3691 RDVTAASKKV---LRESPQS-----ENTATLREKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDM 3762
Cdd:TIGR02168  312 ANLERQLEELeaqLEELESKldelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3763 EQQISRLSMPALRPD-QITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALvaDDDGAKINEILDTDNARYAALRLE 3839
Cdd:TIGR02168  392 ELQIASLNNEIERLEaRLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3840 LRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPLSAL---PQKIREQIED------ND 3896
Cdd:TIGR02168  470 LEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVLSELisvDEGYEAAIEAalggrlQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3897 ALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA---------------VRDIKAKLEKLNNLW-------N 3946
Cdd:TIGR02168  550 VVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvakdLVKFDPKLRKALSYLlggvlvvD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3947 DVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEETLscqeppAAQPQDIKKQQVALQEI 4010
Cdd:TIGR02168  630 DLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEKI------EELEEKIAELEKALAEL 703
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4011 RHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLqnllkflt 4090
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------- 770
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4091 kaEDKFAHLGAVGSDIDAVKRQIEQLKSfkdevdphmvEVEALNRGLKRQAVELTERTspEQAASIREPLSVVNRRWEAL 4170
Cdd:TIGR02168  771 --EEAEEELAEAEAEIEELEAQIEQLKE----------ELKALREALDELRAELTLLN--EEAANLRERLESLERRIAAT 836
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4171 LRGMVERQKQLEHALLHLGQFQHALNELLVWINKtdstldqlkpipgdpqlLEVELAKLKVLANDIQAHQNSV-DTLNDA 4249
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----------------LESELEALLNERASLEEALALLrSELEEL 899
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 386767917  4250 GRQLIETEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALREAH 4299
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
226-322 1.66e-09

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 59.24  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  226 EALLRWARRSTARYpGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK----------------------------ARND 277
Cdd:cd21224     3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAirqpttqtvdraqdeaedfwvaefspstGDSG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767917  278 RPRERLETA---FHIVEKEY----GVTRLLDPEDVDTNEPDEKSLITYISSL 322
Cdd:cd21224    82 LSSELLANEkrnFKLVQQAVaelgGVPALLRASDMSNTIPDEKVVILFLSYL 133
SPEC smart00150
Spectrin repeats;
4737-4839 4.42e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.95  E-value: 4.42e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4737 EKLNARVQALFDWLDHAEHKLRyAKNAPDDEKVSREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIKNW 4816
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDA-EEIEER 78
                            90       100
                    ....*....|....*....|...
gi 386767917   4817 LSIIQQRWEEVRQWAINRESKLE 4839
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2917-3681 1.36e-08

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: 62.00  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2917 ERVKAIREELTNLSKPL---------QSLKALAKDISAEAR---AAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQS 2984
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrleelrEELEELQEELKEAEEeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2985 AATAVS-------QFNEQMKSLGIDLNDLETEIEK-----------LSPPGREIKIVQVQIDDVGKIQTKLDRLVGRLED 3046
Cdd:TIGR02168  293 LANEISrleqqkqILRERLANLERQLEELEAQLEEleskldelaeeLAELEEKLEELKEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3047 AERAADVLVDAgFAADTTQTREQISTLRKTLGRLDNRVRDHEDNlhstlkalrefydhQSQTLDDIQDVSDEFKR--MKP 3124
Cdd:TIGR02168  373 RLEELEEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEaeLKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3125 VGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAGRDLVrsagsgvsttAIEKDLEKLNDRWNDLkERMNERDRRLDV 3204
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----------AAERELAQLQARLDSL-ERLQENLEGFSE 506
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3205 ALLQSGKFQEALAGLSKWLSDT-------EEMVANQKPPSSDYKVVK---AQLQEQKFLKK--------MLLDRQNSMGS 3266
Cdd:TIGR02168  507 GVKALLKNQSGLSGILGVLSELisvdegyEAAIEAALGGRLQAVVVEnlnAAKKAIAFLKQnelgrvtfLPLDSIKGTEI 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3267 LANLGKEVANH-CEPGERASIEKQLNDLMKRFDALTDG---AEqrelDLEEAMEVAKrfhdKISPLELWLdntersVKAM 3342
Cdd:TIGR02168  587 QGNDREILKNIeGFLGVAKDLVKFDPKLRKALSYLLGGvlvVD----DLDNALELAK----KLRPGYRIV------TLDG 652
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3343 ELIPTD----------EEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKVRGVTERYTGLVDA 3412
Cdd:TIGR02168  653 DLVRPGgvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISAL 731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3413 SDNIGALLAESRQGLRHLVLSYQDLVAWMESMEAELKRFKSVpvyAEKLLEQMDHLLELNENIAGHASNVESTVESGAEL 3492
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3493 mkhisNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAlplvqqfHEAHNRLVEWMQSAEAALAPSEPRQAdvlRLEG 3572
Cdd:TIGR02168  809 -----RAELTLLNEEAANLRERLESLERRIAATERRLEDL-------EEQIEELSEDIESLAAEIEELEELIE---ELES 873
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3573 ELADMRPILDSINQvGPQLCQLSPGEGAATIESIvtrdNRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREm 3652
Cdd:TIGR02168  874 ELEALLNERASLEE-ALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE- 947
                          810       820
                   ....*....|....*....|....*....
gi 386767917  3653 DTTLREADLPAMEPKLVRAQLQEHRSIND 3681
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3176-3916 1.46e-08

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: 61.61  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3176 AIEKDLEKLNDRWNDLKERMNERDRRLDVAllqsgkfQEALAGLSKWLSDTEEMV--ANQKPPSSDYKVVKAQLQEQKFL 3253
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEEL-------QKELYALANEISRLEQQKqiLRERLANLERQLEELEAQLEELE 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3254 KKMLLDRQNsmgsLANLGKEVAnhcepgeraSIEKQLNDL---MKRFDALTDGAEQRELDLEEAMEvakRFHDKISPLEL 3330
Cdd:TIGR02168  330 SKLDELAEE----LAELEEKLE---------ELKEELESLeaeLEELEAELEELESRLEELEEQLE---TLRSKVAQLEL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3331 WLDNTERSVKAMeliptdEEKIQQRIREHDRLHDEI--LGKKPDFSDLADVTAQLMHLvsDEEAVNLGEKVRGVTERYtg 3408
Cdd:TIGR02168  394 QIASLNNEIERL------EARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEEL--EEELEELQEELERLEEAL-- 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3409 lvdasDNIGALLAESRQGLRHLVLSYQDLVAWMESMEAELKRFKSvpvYAEKLLEQMDHLLELNeNIAGHAS---NVEST 3485
Cdd:TIGR02168  464 -----EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGLS-GILGVLSeliSVDEG 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3486 VES------GAELMKHISNDEAIQLKDkLDSL-QRRYGDLT------NRGGDLLKSAQNALPLVQQFHEAHNRLVEWMQS 3552
Cdd:TIGR02168  535 YEAaieaalGGRLQAVVVENLNAAKKA-IAFLkQNELGRVTflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3553 AEAALAPSEPRQADVLRLEGELADMRPILDSINQVGPQLCQLSP-----GEGAATIESIVTRDNRRfDSIVEQIQRKAER 3627
Cdd:TIGR02168  614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvitGGSAKTNSSILERRREI-EELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3628 LHLSNQRAKEVTGDIDELLEWFREMDTTLREA--DLPAMEPKLVRAQlQEHRSINDDISSQKGRVRDVTAASKKVLRESP 3705
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELsrQISALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3706 QS-ENTATLREKLDDLKEIVDTVAQLCS---ERLGILEQALP-LSEHFADSHQGLTAWLDDMEQQISRLSMPALRPDQIT 3780
Cdd:TIGR02168  772 EAeEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3781 LQQdknERLLQSIAEHKPLLDKLNKTGEALGALVadddgAKINEILDTDNARYAALRLELRE---RQQALESALQES--- 3854
Cdd:TIGR02168  852 EDI---ESLAAEIEELEELIEELESELEALLNER-----ASLEEALALLRSELEELSEELRElesKRSELRRELEELrek 923
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767917  3855 -SQFSDKLEGMLRALANTVDQVNQ-----LDPLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAA 3916
Cdd:TIGR02168  924 lAQLELRLEGLEVRIDNLQERLSEeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
223-328 2.24e-08

second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409163  Cd Length: 115  Bit Score: 55.46  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21314    11 TPKQRLLGWIQN---KVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                          90       100
                  ....*....|....*....|....*..
gi 386767917  302 PEDVDTNEPDEKSLITYISSlydvFPE 328
Cdd:cd21314    88 PEEIVDPNVDEHSVMTYLSQ----FPK 110
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5229-5457 3.58e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 60.57  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5229 STPNAAATASSSPHAHNGGSSN---LPPYMSGQGPIIKVRERSVRSIP-----MSRPSRSSLSASTPDSLSDNEGSHGGP 5300
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPpaaASPRPPRRSSPISASASSPAPAPgrsaaDDAGASSSDSSSSESSGCGWGPENECP 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5301 SGRYTPrKVTYTSTRTGLTPG--GSRAGSKPNSRPLSRQGSKPPSRHGSTLSLDSTDDHTPSRIPQRKPSTGST-ASGTT 5377
Cdd:PHA03307  257 LPRPAP-ITLPTRIWEASGWNgpSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTsSSSES 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5378 PRPArlsvtttttpgsrlngtstitrkTASGSASPAPTRRNISGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPTEKR 5457
Cdd:PHA03307  336 SRGA-----------------------AVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARA 392
SPEC smart00150
Spectrin repeats;
3746-3848 4.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 4.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3746 EHFADSHQGLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3825
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 386767917   3826 LDTDNARYAALRLELRERQQALE 3848
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3211-3312 5.25e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 5.25e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3211 KFQEALAGLSKWLSDTEEMVAnQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPgERASIEKQL 3290
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 386767917   3291 NDLMKRFDALTDGAEQRELDLE 3312
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3969-4068 7.10e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 7.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3969 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 4048
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 386767917   4049 DLDNAWDNITALYAKREENL 4068
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
471-689 7.13e-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: 56.30  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  471 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 543
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  544 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 623
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  624 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 689
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1047-1250 1.26e-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: 55.53  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1047 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1122
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1123 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1196
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386767917 1197 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1250
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
221-328 1.27e-07

second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409162  Cd Length: 110  Bit Score: 53.17  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  221 NVSAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRL 299
Cdd:cd21313     6 KQTPKQRLLGWIQN---KIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQV 82
                          90       100
                  ....*....|....*....|....*....
gi 386767917  300 LDPEDVDTNEPDEKSLITYISSlydvFPE 328
Cdd:cd21313    83 ITPEEIIHPDVDEHSVMTYLSQ----FPK 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3504-4348 2.51e-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: 57.76  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3504 LKDKLDSLQR------RYGDLTNRggdlLKSAQNALpLVQQFHEAHNRLVEWMQSAEAALAPSEPRQADVLRLEGELADM 3577
Cdd:TIGR02168  198 LERQLKSLERqaekaeRYKELKAE----LRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3578 RPILDSINqvgpqlcqlspgEGAATIESIVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgdiDELLEWFREMDTTlr 3657
Cdd:TIGR02168  273 RLEVSELE------------EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDEL-- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3658 EADLPAMEPKLvrAQLQEhrsinddissqkgrvrDVTAASKKVLRESPQSENtatLREKLDDLKEIVDTVAqlcSERLGI 3737
Cdd:TIGR02168  336 AEELAELEEKL--EELKE----------------ELESLEAELEELEAELEE---LESRLEELEEQLETLR---SKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3738 LEQALPLSEhfadshqgltawlddmeqQISRLSmpalrpDQITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALva 3815
Cdd:TIGR02168  392 ELQIASLNN------------------EIERLE------ARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL-- 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3816 DDDGAKINEILDTDNARYAALRLELRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPL 3881
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVL 525
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3882 SAL---PQKIREQIED------NDALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA-------------- 3930
Cdd:TIGR02168  526 SELisvDEGYEAAIEAalggrlQAVVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvak 605
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3931 -VRDIKAKLEKLNNLW-------NDVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEET 3986
Cdd:TIGR02168  606 dLVKFDPKLRKALSYLlggvlvvDDLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEK 685
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3987 LscqeppAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREE 4066
Cdd:TIGR02168  686 I------EELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4067 NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAHLGAvgsDIDAVKRQIEQLKSFKDEVDPhmvEVEALNRGLKRQAVELTE 4146
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEA---QIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLES 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4147 RTspEQAASIREPLSVVNRRWEALLrgmvERQKQLEHALLHLGQFQHALN-ELLVWINKTDSTLDQLKPIPGDPQLLEVE 4225
Cdd:TIGR02168  829 LE--RRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELEsELEALLNERASLEEALALLRSELEELSEE 902
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4226 LAKL--KVLANDiQAHQNSVDTLNDAGRQLIETEkgsVEASTTQEklrKLNNEWKQLLQKASDRQHELEEALREAHGYIA 4303
Cdd:TIGR02168  903 LRELesKRSELR-RELEELREKLAQLELRLEGLE---VRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|....*
gi 386767917  4304 EVQDILGWLGDVDavigaskpvgglpETATEQLERFMEVYNELDE 4348
Cdd:TIGR02168  976 RLENKIKELGPVN-------------LAAIEEYEELKERYDFLTA 1007
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
690-783 2.53e-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: 51.94  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   690 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 769
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 386767917   770 TALQQQWAWLLQLT 783
Cdd:pfam00435   83 EELNERWEQLLELA 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2528-3366 2.83e-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: 57.37  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2528 EIKLKDILGKWDDLVGKLDDRANSLGGAADS-------SKEFDAAVNRLREALQNISDNLDTLptDGDHQENLRKIENLE 2600
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEEleeltaeLQELEEKLEELRLEVSELEEEIEEL--QKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2601 RQLEGQRPLLADVEQSAATLCNILGDPASRAD-VNSRVAALEKQYLALQKKLDTKKAETEAslrdgrhfaencsktlgwL 2679
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEELESLEAELEE------------------L 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2680 GGELSNLTDRLLvsahkpTLQHQIDTHEP----IYREVMAREHEVIMLINKGKDLTDRQQ----------DRGVKRDLDR 2745
Cdd:TIGR02168  364 EAELEELESRLE------ELEEQLETLRSkvaqLELQIASLNNEIERLEARLERLEDRRErlqqeieellKKLEEAELKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2746 IQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRDLQTFRSEVWKHSGE 2825
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2826 FENTKGLgetflsscdidkepiKAELQDIRDRWER-LNNDLIARAHEIenCSRRLDDFNDELRNL-DHSLGRCEdrLAAH 2903
Cdd:TIGR02168  518 LSGILGV---------------LSELISVDEGYEAaIEAALGGRLQAV--VVENLNAAKKAIAFLkQNELGRVT--FLPL 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2904 DALGGAAKDPKLLERvkaireeLTNLSKPLQSLKALAKdISAEARAAGGDADHLTSEVDGLADRMsELQGRLDDRC---- 2979
Cdd:TIGR02168  579 DSIKGTEIQGNDREI-------LKNIEGFLGVAKDLVK-FDPKLRKALSYLLGGVLVVDDLDNAL-ELAKKLRPGYrivt 649
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2980 --GELQSAATAVSQfneqmKSLGIDLNDLET--EIEKLSppgREIKIVQVQIDDvgkIQTKLDRLVGRLEDAERAADVLV 3055
Cdd:TIGR02168  650 ldGDLVRPGGVITG-----GSAKTNSSILERrrEIEELE---EKIEELEEKIAE---LEKALAELRKELEELEEELEQLR 718
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3056 dagfaADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKpvgselDQIRRQ 3135
Cdd:TIGR02168  719 -----KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEEL 787
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3136 QEDFRNFRERkveplainvdkvnvagrdlvrsagsgvsTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEA 3215
Cdd:TIGR02168  788 EAQIEQLKEE----------------------------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3216 LAGLSKWLSDTEEMVANQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcepgERASIEKQLNDLMK 3295
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE----ELRELESKRSELRR 915
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767917  3296 RFDALTDGAEQRELDLEEAMEVAKRFHDKISplELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEI 3366
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4037-4371 3.63e-07

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: 57.00  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4037 EPDK-PEVKKHIEDLDNAWDNITALYAKREE---NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAH-LGAVGSDIDAVKR 4111
Cdd:TIGR02169  672 EPAElQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4112 QIEQLKSFKDEVDPHMVEVEALNRGLKRQAVELTERTSPEQAASIREPLSVVN---RRWEALLRGmVERQKQLEHALLHL 4188
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEeevSRIEARLRE-IEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4189 GQ--FQHALNELLVWINKTDSTLDQLKPIPGDPQLLEVELAKLKVLANDIQA-HQNSVDTLNDAGRQLIETEKGSVEAST 4265
Cdd:TIGR02169  831 LEkeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrLGDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4266 TQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEVQDilgwLGDVDAV-------IGASKPVGGLpetATEQLER 4338
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAElqrveeeIRALEPVNML---AIQEYEE 983
                          330       340       350
                   ....*....|....*....|....*....|...
gi 386767917  4339 FMEVYNELDENRPKVETIQAQGQEYIKRQNQMK 4371
Cdd:TIGR02169  984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2308-3080 4.13e-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: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2308 SELSPVQQQLSEinnrygligvrLNDRQHELDNLNEELRKQYENLKGLAQFLE-RIQRQlpkesVSNKDEAERCIKQARK 2386
Cdd:TIGR02168  260 AELQELEEKLEE-----------LRLEVSELEEEIEELQKELYALANEISRLEqQKQIL-----RERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2387 ILEDMYEKQSLLDTTKAQVKDILrrksdvpgaEQLRQENDSIQEKWKNLNDICKNRIAFSEKLRDFLDThgnLKSWLDSK 2466
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKL---------EELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2467 ERMLTVL-GPISS-DPRMVQSQVQQVQVLRE-EFRTQQPQLKHFQELGHDVVDHLAGTPDAQAVEIKLKDILGKWDDLVG 2543
Cdd:TIGR02168  392 ELQIASLnNEIERlEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2544 KLDDRANSLggaadsSKEFDAAVNRLrEALQNISDNLDTLptdgdhQENLRKIENLERQLEGQRPLLAD---VEQS---- 2616
Cdd:TIGR02168  472 EAEQALDAA------ERELAQLQARL-DSLERLQENLEGF------SEGVKALLKNQSGLSGILGVLSElisVDEGyeaa 538
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2617 -AATLCNILGDPASR--ADVNSRVAALEKQ------YLALQ----KKLDTKKAETEASLRDGRHFAENCSKTLGWLGGEL 2683
Cdd:TIGR02168  539 iEAALGGRLQAVVVEnlNAAKKAIAFLKQNelgrvtFLPLDsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2684 SNLTDRLLVSAHKPTLQHQIDTHEPIYREVMArEHEVIM---LINKGKDLTDrQQDRGVKRDLDRIQQQWEKLRREAVDR 2760
Cdd:TIGR02168  619 SYLLGGVLVVDDLDNALELAKKLRPGYRIVTL-DGDLVRpggVITGGSAKTN-SSILERRREIEELEEKIEELEEKIAEL 696
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2761 HTRLQTcmehCKKYSQTSETFLAWLRTA-EDKLADLTPGVLSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETflss 2839
Cdd:TIGR02168  697 EKALAE----LRKELEELEEELEQLRKElEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE---- 768
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2840 cdiDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDP--KLLE 2917
Cdd:TIGR02168  769 ---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRleDLEE 845
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2918 RVKAIREELTNLSKPLQSLKALAKDISAEaraaggdADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMK 2997
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2998 SLGIDLNDLETEIEKLSppgreikivqvqiddvGKIQTKLDRLVGRLEDAERAADVLVdAGFAADTTQTREQISTLRKTL 3077
Cdd:TIGR02168  919 ELREKLAQLELRLEGLE----------------VRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKI 981

                   ...
gi 386767917  3078 GRL 3080
Cdd:TIGR02168  982 KEL 984
SPEC smart00150
Spectrin repeats;
3641-3739 4.34e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 4.34e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3641 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3720
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEERLEEL 82
                            90
                    ....*....|....*....
gi 386767917   3721 KEIVDTVAQLCSERLGILE 3739
Cdd:smart00150   83 NERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3320-3420 5.18e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 5.18e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3320 RFHDKISPLELWLDNTERSVKAMElIPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGEKV 3399
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   3400 RGVTERYTGLVDASDNIGALL 3420
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
359-685 8.28e-07

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: 55.84  E-value: 8.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   359 REKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYFETVGEVDVEAELrpdaiekawyrmn 438
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------- 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   439 taLQDREvilQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEGRRIERLhpvdaKSIVEALETEIRHleEPIQD 518
Cdd:TIGR02169  728 --LEQEE---EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-----EEALNDLEARLSH--SRIPE 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   519 MNQ------DCHVLNEGRyphVSELHKKVNKLHQRWAQLRtnfhtnlvQKLSGLKYPVHETTVTRQTRmvvESRQIDTNP 592
Cdd:TIGR02169  796 IQAelskleEEVSRIEAR---LREIEQKLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSI---EKEIENLNG 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   593 HFRDLQEHIEWCQNKLKQLlaADYGSDLPSVKEELDRQQHEHKI-IDQFHTKIlNDERQQTKFSGDELALYQQRLNQLQK 671
Cdd:TIGR02169  862 KKEELEEELEELEAALRDL--ESRLGDLKKERDELEAQLRELERkIEELEAQI-EKKRKRLSELKAKLEALEEELSEIED 938
                          330
                   ....*....|....
gi 386767917   672 VYAELLSTSTKRLS 685
Cdd:TIGR02169  939 PKGEDEEIPEEELS 952
SPEC smart00150
Spectrin repeats;
2773-2873 8.50e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 8.50e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   2773 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2852
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   2853 DIRDRWERLNNDLIARAHEIE 2873
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2848-3123 9.48e-07

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: 55.84  E-value: 9.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2848 KAELQDIRDRWERLNNDLIARAHEIEN-------CSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVK 2920
Cdd:TIGR02169  715 SRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2921 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMK--- 2997
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEele 874
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2998 ----SLGIDLNDLETEIEKLSPPGREIKIVQVQIDdvGKIQTKLDRLVGRLEDAERAADVL--VDAGFAADTTQTREQIS 3071
Cdd:TIGR02169  875 aalrDLESRLGDLKKERDELEAQLRELERKIEELE--AQIEKKRKRLSELKAKLEALEEELseIEDPKGEDEEIPEEELS 952
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767917  3072 --TLRKTLGRLDNRVRDHED-NL------HSTLKALREfYDHQSQTL----DDIQDVSDEFKRMK 3123
Cdd:TIGR02169  953 leDVQAELQRVEEEIRALEPvNMlaiqeyEEVLKRLDE-LKEKRAKLeeerKAILERIEEYEKKK 1016
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2915-3145 9.85e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2915 LLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVD--GLADRMSELQGRLDdrcgELQSAATAVSQF 2992
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELE----RLDASSDDLAAL 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2993 NEQMKSLGIDLNDLETEIEKLSppgREIKIVQVQIDDvgkIQTKLDRLVGRLEDAERAADVLVDAGF------AADTTQT 3066
Cdd:COG4913   691 EEQLEELEAELEELEEELDELK---GEIGRLEKELEQ---AEEELDELQDRLEAAEDLARLELRALLeerfaaALGDAVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3067 REQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLD-DIQDVsDEFKRMkpvgseLDQIR-----RQQEDFR 3140
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDaDLESL-PEYLAL------LDRLEedglpEYEERFK 837

                  ....*
gi 386767917 3141 NFRER 3145
Cdd:COG4913   838 ELLNE 842
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
223-320 1.01e-06

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 50.55  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWrkaRNDRPRERLET---AFHIVEKEYGVTR 298
Cdd:cd21315    16 TPKQRLLGWIQ---SKVPDLPITNFTNDWNDGKAIGALVDALAPGLCpDW---EDWDPKDAVKNakeAMDLAEDWLDVPQ 89
                          90       100
                  ....*....|....*....|..
gi 386767917  299 LLDPEDVDTNEPDEKSLITYIS 320
Cdd:cd21315    90 LIKPEEMVNPKVDELSMMTYLS 111
SPEC smart00150
Spectrin repeats;
3099-3203 1.16e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3099 REFYDHQSQTLDDIQDVsDEFKRMKPVGSELDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAIE 3178
Cdd:smart00150    1 QQFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAF-EAELEAHEERVEALNELGEQLIEE--GHPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 386767917   3179 KDLEKLNDRWNDLKERMNERDRRLD 3203
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2843-3153 1.32e-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: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2843 DKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAahdalggaakdpKLLERVKAI 2922
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE------------EAEEELAEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2923 REELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGID 3002
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3003 LNDLETEIEKLSppgREIKIVQVQID----DVGKIQTKLDRLVGRLEDAERAADVLVDagfaaDTTQTREQISTLRKTLG 3078
Cdd:TIGR02168  861 IEELEELIEELE---SELEALLNERAsleeALALLRSELEELSEELRELESKRSELRR-----ELEELREKLAQLELRLE 932
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917  3079 RLDNRVRdhednlhSTLKALREFYdhqSQTLDDIQdvsdefKRMKPVGSELDQIRRQQEDFRNFRER--KVEPLAIN 3153
Cdd:TIGR02168  933 GLEVRID-------NLQERLSEEY---SLTLEEAE------ALENKIEDDEEEARRRLKRLENKIKElgPVNLAAIE 993
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4407-4511 2.19e-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: 49.24  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4407 KEATEFHDTLQAFVEWLTQAEKLLSNaEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKYfSQKQDVILI 4486
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 386767917  4487 KNLLVSVQHRWERVVSKAAERTRAL 4511
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
2666-2765 2.46e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.25  E-value: 2.46e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   2666 RHFAENCSKTLGWLGGELSNLTDRLlVSAHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2743
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAeeIEERL 79
                            90       100
                    ....*....|....*....|..
gi 386767917   2744 DRIQQQWEKLRREAVDRHTRLQ 2765
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4632-4730 2.91e-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: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4632 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSGN--NPEVGRQLD 4709
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHyaSEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 386767917  4710 EMQSIWEEVKSAVAKRGERLQ 4730
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
3856-3960 3.26e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 3.26e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3856 QFSDKLEGMLRALANTVDQVNQlDPLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIakagNKADPAVRDIK 3935
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI----EEGHPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 386767917   3936 AKLEKLNNLWNDVQNATKKRGSSLD 3960
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2803-3203 6.70e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.73  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2803 AKLETRLRDLQTFRSEVwkhSGEFENTKGLGETFLSSCDiDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDF 2882
Cdd:PRK02224  202 KDLHERLNGLESELAEL---DEEIERYEEQREQARETRD-EADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2883 NDELRNLDHSLGRCEDRLAahDALGGAAKDPKLLERVKAIREELtnlSKPLQSLKALAKDISAEARAAGGDADHLTSEVD 2962
Cdd:PRK02224  278 AEEVRDLRERLEELEEERD--DLLAEAGLDDADAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2963 GLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSL--------------GIDLNDLETEIEKLSPPGREIKivqvqiD 3028
Cdd:PRK02224  353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELeeeieelrerfgdaPVDLGNAEDFLEELREERDELR------E 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3029 DVGKIQTKLDRLVGRLEDAERAADV---------LVDAGFAADTTQTREQISTLRKTLGRLDNRVRDHE----------- 3088
Cdd:PRK02224  427 REAELEATLRTARERVEEAEALLEAgkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEerleraedlve 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3089 -----DNLHSTLKALREFYDHQSQTLDDIQDVSDEF-KRMKPVGSELDQIRRQQEDFRNFRERKVEPLA-INVDKVNVAG 3161
Cdd:PRK02224  507 aedriERLEERREDLEELIAERRETIEEKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAeLNSKLAELKE 586
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 386767917 3162 R--DLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLD 3203
Cdd:PRK02224  587 RieSLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA 630
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
5054-5123 6.95e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5054 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5123
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3283-3974 7.28e-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: 52.75  E-value: 7.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3283 RASIEKQLNDL------MKRFDALTDgaEQRELDLEEAMEVAKRFHDKISPLELWLDNTERSVKAME-LIPTDEEKIQQR 3355
Cdd:TIGR02168  195 LNELERQLKSLerqaekAERYKELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTaELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3356 IREHDRLHDEILGKKPDF----SDLADVTAQLMHLvsDEEAVNLGEKVRGVTERYTGLVDASDNIGALLAESRQGLrhlv 3431
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELyalaNEISRLEQQKQIL--RERLANLERQLEELEAQLEELESKLDELAEELAELEEKL---- 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3432 lsyQDLVAWMESMEAELKRFKsvpvyaEKLLEQMDHLLELNENIAGHASNVESTVESGAELMKHISNdeaiqLKDKLDSL 3511
Cdd:TIGR02168  347 ---EELKEELESLEAELEELE------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-----LEARLERL 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3512 QRRYGDLTNRGGDLLKSAQNA-LPLVQQFHEAHNRLVEWMQSAEAALAPSEPRQADVLR--------LEGELADMRPILD 3582
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEeaeqaldaAERELAQLQARLD 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3583 SINQ-------------------------VGPQLCQLSPGEG---------AATIESIVTRDN----RRFDSIVEQIQRK 3624
Cdd:TIGR02168  493 SLERlqenlegfsegvkallknqsglsgiLGVLSELISVDEGyeaaieaalGGRLQAVVVENLnaakKAIAFLKQNELGR 572
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3625 AERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADLPAMEPKLVRAQLQEHRSINDDI-------SSQKGRVRDVTAAS 3697
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLdnalelaKKLRPGYRIVTLDG 652
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3698 KKVLRE---SPQSENTATL----REKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDMEQQISRLS 3770
Cdd:TIGR02168  653 DLVRPGgviTGGSAKTNSSilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3771 MPALR--------PDQITLQQDKNERLLQSIAEhkpLLDKLNKTGEALGALVAD------------DDGAKINEILDTDN 3830
Cdd:TIGR02168  733 KDLARleaeveqlEERIAQLSKELTELEAEIEE---LEERLEEAEEELAEAEAEieeleaqieqlkEELKALREALDELR 809
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3831 ARYAALRLELRERQQALESALQESSQFSDKLEGMLRALANTVDQV-------------------------NQLDPLSALP 3885
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleelieeleseleallNERASLEEAL 889
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3886 QKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSV 3965
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969

                   ....*....
gi 386767917  3966 AEPFWKQLN 3974
Cdd:TIGR02168  970 ARRRLKRLE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2590-3358 9.30e-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: 52.37  E-value: 9.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2590 QENLRKIENLERQLEGQ-RPLLADVEQsaatlcnilgdpASR-ADVNSRVAALEKQYLALQKK-LDTKKAETEASLRDGR 2666
Cdd:TIGR02168  185 RENLDRLEDILNELERQlKSLERQAEK------------AERyKELKAELRELELALLVLRLEeLREELEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2667 HFAENCSKTLGWLGGELSNLtdRLLVSAHKPTLQHQIDTHEPIYREVMAREHEvIMLINKGKDLTDRQQDRgVKRDLDRI 2746
Cdd:TIGR02168  253 EELEELTAELQELEEKLEEL--RLEVSELEEEIEELQKELYALANEISRLEQQ-KQILRERLANLERQLEE-LEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2747 QQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAK------------------LETR 2808
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqlelqiaslnneierLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2809 LRDLQTfRSEVWKHSGEfENTKGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRN 2888
Cdd:TIGR02168  409 LERLED-RRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2889 LDHSLGRCEDRLAAHDALGGAAKDpkllerVKAIREELTNLSKPL-QSLKALAKDISAEARAAGGDADHLTseVDGLADR 2967
Cdd:TIGR02168  487 LQARLDSLERLQENLEGFSEGVKA------LLKNQSGLSGILGVLsELISVDEGYEAAIEAALGGRLQAVV--VENLNAA 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2968 MSELQGRLDDRCG-----ELQSAATAVSQFNEQMKSLGID-----LNDLETEIEKLSPPGREIkIVQVQIDDVGKIQTKL 3037
Cdd:TIGR02168  559 KKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREILKNIEgflgvAKDLVKFDPKLRKALSYL-LGGVLVVDDLDNALEL 637
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3038 DRLVGRLEDAERAADVLVDAGFAAdTTQTREQISTL---RKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLDDIQD 3114
Cdd:TIGR02168  638 AKKLRPGYRIVTLDGDLVRPGGVI-TGGSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3115 VSDEFKRMKpvgselDQIRRQQEDFRNFrERKVEPLAinvDKVNVAGRDLVRSAgsgVSTTAIEKDLEKLNDRWNDLKER 3194
Cdd:TIGR02168  717 LRKELEELS------RQISALRKDLARL-EAEVEQLE---ERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAE 783
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3195 MNERDRRLDVALLQSGKFQEALAGLSKWLSDTEEMVANQKppsSDYKVVKAQLQEQKFLKKMLLDRQNSM-GSLANLGKE 3273
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELsEDIESLAAE 860
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3274 VANHCEPGERasIEKQLNDLMKRFDALTDGAEQRELDLEEAMEVAKRFHDKISPLELWLDNTERSVKAMELiptDEEKIQ 3353
Cdd:TIGR02168  861 IEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLE 935

                   ....*
gi 386767917  3354 QRIRE 3358
Cdd:TIGR02168  936 VRIDN 940
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2739-3454 1.03e-05

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: 52.38  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2739 VKRDLDRIQQQWEKLR---REAVDRHTRLQTCMEHCKKYSqtsetflawlrtaedkladltpgvlskaKLETRLRDLqtf 2815
Cdd:TIGR02169  175 ALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQ----------------------------ALLKEKREY--- 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2816 rsEVWKHSGEFENT---KGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDL---------------------IARAH- 2870
Cdd:TIGR02169  224 --EGYELLKEKEALerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnkkikdlgeeeqlrvkekIGELEa 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2871 EIENCSRRLDDFNDELRNLDHSLGRCEDRL----AAHDALGGAAKDPKLleRVKAIREELTNLSKPLQSLKALAKDISAE 2946
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIdkllAEIEELEREIEEERK--RRDKLTEEYAELKEELEDLRAELEEVDKE 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2947 ARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETE----IEKLSPPGREIKI 3022
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedkALEIKKQEWKLEQ 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3023 VQVQIDDVGK----IQTKLDRLVGRLEDAER-------AADVLVDA--GFAADTTQTREQISTLRKTL------------ 3077
Cdd:TIGR02169  460 LAADLSKYEQelydLKEEYDRVEKELSKLQRelaeaeaQARASEERvrGGRAVEEVLKASIQGVHGTVaqlgsvgeryat 539
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3078 -------GRLDNRVRDHEDNLHSTLKALREfydHQSQTLDDIqdvsdEFKRMKPVGSELDQIRRQQE-----DFRNFrER 3145
Cdd:TIGR02169  540 aievaagNRLNNVVVEDDAVAKEAIELLKR---RKAGRATFL-----PLNKMRDERRDLSILSEDGVigfavDLVEF-DP 610
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3146 KVEP--------------------LAINVDKVNVAGrDLV----------RSAGSGVSTTAIEK--------DLEKLNDR 3187
Cdd:TIGR02169  611 KYEPafkyvfgdtlvvedieaarrLMGKYRMVTLEG-ELFeksgamtggsRAPRGGILFSRSEPaelqrlreRLEGLKRE 689
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3188 WNDLKERMNERDRRLDVALL---------------------QSGKFQEALAGLSKWLSDTEEMVANQKPPSSDYKVVKAQ 3246
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQelsdasrkigeiekeieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3247 LQEQKF--------LKKMLLDR--QNSMGSLANLGKEVANhcEPGERASIEKQLNDLmkrfdaltdgaEQRELDLEEAME 3316
Cdd:TIGR02169  770 LEEDLHkleealndLEARLSHSriPEIQAELSKLEEEVSR--IEARLREIEQKLNRL-----------TLEKEYLEKEIQ 836
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3317 vakrfhDKISPLELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEILGKKPDFS-DLADVTAQLMHLVSDEEAVN- 3394
Cdd:TIGR02169  837 ------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKkERDELEAQLRELERKIEELEa 910
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917  3395 -LGEKVRGVTERYTGLVDASDNIGALLAESRQGLR--HLVLSYQDLVAWMESMEAELKRFKSV 3454
Cdd:TIGR02169  911 qIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRALEPV 973
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2330-3316 1.20e-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: 52.37  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2330 RLNDRQHELDNLN---EELRKQYENLKGLAQFLERIQ------RQLPKE-SVSNKDEAERCIKQARKILEDMYEK----Q 2395
Cdd:TIGR02168  180 KLERTRENLDRLEdilNELERQLKSLERQAEKAERYKelkaelRELELAlLVLRLEELREELEELQEELKEAEEEleelT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2396 SLLDTTKAQVkDILRRKSdvpgaEQLRQENDSIQEKWKNLN---DICKNRIAF-SEKLRDFLDTHGNLKSWLDSKERMLt 2471
Cdd:TIGR02168  260 AELQELEEKL-EELRLEV-----SELEEEIEELQKELYALAneiSRLEQQKQIlRERLANLERQLEELEAQLEELESKL- 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2472 vlgpissdprmvqsqvqqvQVLREEFRTQQPQLKHFQElghdvvdhlagtpDAQAVEIKLKDILGKWDDLVGKLDDRAns 2551
Cdd:TIGR02168  333 -------------------DELAEELAELEEKLEELKE-------------ELESLEAELEELEAELEELESRLEELE-- 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2552 lggaadssKEFDAAVNRLREALQNISDNLDTLptdgdhQENLRKIENLERQLEGQRPLLADVEQSAatlcnilgDPASRA 2631
Cdd:TIGR02168  379 --------EQLETLRSKVAQLELQIASLNNEI------ERLEARLERLEDRRERLQQEIEELLKKL--------EEAELK 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2632 DVNSRVAALEKQYLALQKKLDTKKAEtEASLRDGRHFAENcsktlgwlggelsnltDRLLVSAHKPTLQHQIDTHEPIYR 2711
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEA-LEELREELEEAEQ----------------ALDAAERELAQLQARLDSLERLQE 499
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2712 EVMAREHEVIMLINKGKDLTDrqqDRGVKRDLDRIQQQWEKlRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWlrTAEDK 2791
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSGLSG---ILGVLSELISVDEGYEA-AIEAALGGRLQAVVVENLNAAKKAIA-FLKQ--NELGR 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2792 LADLTPGVLSKAKLEtrlrdlqtfrsevwkhsGEFENTKGLGETFLSSCDidkepikaELQDIRDRWERLNNDLIARAHE 2871
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQ-----------------GNDREILKNIEGFLGVAK--------DLVKFDPKLRKALSYLLGGVLV 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2872 IENcsrrLDDFNDELRNLDHSL------GrceDRLAAHDALGGAAKDPK--LLERvkaiREELTNLSKPLQSLKALAKDI 2943
Cdd:TIGR02168  628 VDD----LDNALELAKKLRPGYrivtldG---DLVRPGGVITGGSAKTNssILER----RREIEELEEKIEELEEKIAEL 696
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2944 SAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEKLSppgreikiv 3023
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE--------- 767
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3024 qvqiDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYD 3103
Cdd:TIGR02168  768 ----ERLEEAEEELAEAEAEIEELE------------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3104 HQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAgRDLVRSAGSGVSTT--AIEKDL 3181
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-LALLRSELEELSEElrELESKR 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3182 EKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLskwLSDTEEMVANQKPpssdyKVVKAQLQEQKFLKKmlLDRQ 3261
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALEN-----KIEDDEEEARRRLKR--LENK 980
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386767917  3262 nsmgsLANLGkevanhcePGERASIEkQLNDLMKRFDALTdgaEQRElDLEEAME 3316
Cdd:TIGR02168  981 -----IKELG--------PVNLAAIE-EYEELKERYDFLT---AQKE-DLTEAKE 1017
SPEC smart00150
Spectrin repeats;
1961-2065 1.36e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.36e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   1961 QGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVE 2040
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD--AEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 386767917   2041 SNLNDVTVKFEKLYEKANKRGEFLD 2065
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
343-552 1.84e-05

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: 49.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  343 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 422
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  423 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 502
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767917  503 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 552
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2907-3320 2.13e-05

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: 51.22  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2907 GGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAA 2986
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2987 TAVSQFNEQMKSLGIDLNDLETEIEKLsppgreIKIVQVQIDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaadTTQT 3066
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKEL------EARIEELEEDLHKLEEALNDLEARLSHSR--------------IPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3067 REQISTLRKTLGRLDNRVRDHEDNLHStLKALREFYDHQSQTLDDIQDVSDEFKRMkpvgseldqIRRQQEDFRNFRERK 3146
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKS---------IEKEIENLNGKKEEL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3147 VEPLAinvdKVNVAGRDLVRSAGSgvsttaIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDT 3226
Cdd:TIGR02169  867 EEELE----ELEAALRDLESRLGD------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3227 EEMVANQKPPSS---DYKVVKAQLQEqkflkkmLLDRQNSMGSLANLGKEvanhcepgERASIEKQLNDLMKRFDALTdg 3303
Cdd:TIGR02169  937 EDPKGEDEEIPEeelSLEDVQAELQR-------VEEEIRALEPVNMLAIQ--------EYEEVLKRLDELKEKRAKLE-- 999
                          410
                   ....*....|....*...
gi 386767917  3304 AEQREL-DLEEAMEVAKR 3320
Cdd:TIGR02169 1000 EERKAIlERIEEYEKKKR 1017
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3641-3740 2.22e-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: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3641 DIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPQSenTATLREKLDDL 3720
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 386767917  3721 KEIVDTVAQLCSERLGILEQ 3740
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2452-2552 2.60e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 2.60e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   2452 FLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAVEIKL 2531
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   2532 KDILGKWDDLVGKLDDRANSL 2552
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1628-2186 4.09e-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: 50.44  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1628 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1693
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1694 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1767
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1768 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1845
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1846 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1901
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1902 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1960
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1961 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 2011
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2012 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2082
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2083 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2158
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 386767917  2159 INISIDERAKLSKQKAEQQLAYEGLKDQ 2186
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
EF-hand_7 pfam13499
EF-hand domain pair;
5052-5116 4.53e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 4.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917  5052 KSRLTDLFRKMDKDNNGMIPRDVFIDGI--LNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5116
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1571-2189 4.92e-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: 50.06  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1571 LEVIQREISEAESGYETAEKRiKQAVFEKFNMCEENVNDLLKWVTTVEQKISsvggprEKIDELRNQINALKQIKDEIES 1650
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELE------ELEAELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1651 QQRPVATCLEQIRQIvltggdvlsAPEVTTLENSGRELRSRVDRVNDRTVRLLRRLEAG------------RDELTKLRS 1718
Cdd:TIGR02168  384 LRSKVAQLELQIASL---------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQE 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1719 ELDVFSDWLQVARRTLEDKERSL----SDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKF------------VDES 1782
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALdaaeRELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisVDEG 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1783 KEfLAILndfrTSLPERLPHVepLSSAESPIRQEvslVSAQYKDLLNRVNALQdrVSGLGGRQREYQDALDKANewlrsv 1862
Cdd:TIGR02168  535 YE-AAIE----AALGGRLQAV--VVENLNAAKKA---IAFLKQNELGRVTFLP--LDSIKGTEIQGNDREILKN------ 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1863 HPRVSRIISEPIAGDPKgvqdqmneAKALHNELLSSGRLVDNAQQALdNLLRSLG--------------------GQLSP 1922
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPK--------LRKALSYLLGGVLVVDDLDNAL-ELAKKLRpgyrivtldgdlvrpggvitGGSAK 667
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1923 MEINQLEL--PIADLKNNYQQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIKERLQEQIR 2000
Cdd:TIGR02168  668 TNSSILERrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI--SALRKDLARLEAEVEQL 745
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2001 EHKVllADLQSHQASIDSVQVSAKHLLASASNARIAkkVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRLSRYLDEIST 2080
Cdd:TIGR02168  746 EERI--AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2081 VEQRMASLQEALDSRETSLLSTEELARRMNElsrDKDQLAPQFEDCVRSGKDLIS-------LRDVTDTGV--LRDRIKA 2151
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESeleallnERASLEEALalLRSELEE 898
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 386767917  2152 LESQWRNINISI----DERAKLSKQKAEQQLAYEGLKDQVLS 2189
Cdd:TIGR02168  899 LSEELRELESKRselrRELEELREKLAQLELRLEGLEVRIDN 940
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
5054-5116 6.12e-05

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: 43.69  E-value: 6.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767917 5054 RLTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5116
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3211-3313 6.41e-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: 45.00  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3211 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcEPGERASIEKQL 3290
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 386767917  3291 NDLMKRFDALTDGAEQRELDLEE 3313
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4735-4840 6.86e-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: 45.00  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4735 DAEKLNARVQALFDWLDHAEHKLRyAKNAPDDEKVSREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIK 4814
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 386767917  4815 NWLSIIQQRWEEVRQWAINRESKLEQ 4840
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
2594-3375 8.05e-05

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: 49.66  E-value: 8.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2594 RKIE--NLERQLEGQRPLLADVEQSAATLcnilgdPASRADVNSRVAALEKQYLALQKKLDT--KKAETEASLRDG---- 2665
Cdd:TIGR00606  326 RELEklNKERRLLNQEKTELLVEQGRLQL------QADRHQEHIRARDSLIQSLATRLELDGfeRGPFSERQIKNFhtlv 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2666 RHFAENCSKTLGWLggeLSNLTDRLlvsahkPTLQHQIDTHE--------PIYREVMAREHEVIMLINKGKDLtdrQQDR 2737
Cdd:TIGR00606  400 IERQEDEAKTAAQL---CADLQSKE------RLKQEQADEIRdekkglgrTIELKKEILEKKQEELKFVIKEL---QQLE 467
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2738 GVKRDLDRIQQQWEKLRRE--AVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRD---- 2811
Cdd:TIGR00606  468 GSSDRILELDQELRKAERElsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkmdk 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2812 LQTFRSEVWKHS-------GEFENTKGLGETFLSscdidkepIKAELQDIRDRWERLNNDLiARAHEIENcsrrldDFND 2884
Cdd:TIGR00606  548 DEQIRKIKSRHSdeltsllGYFPNKKQLEDWLHS--------KSKEINQTRDRLAKLNKEL-ASLEQNKN------HINN 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2885 ELRNLDHSLGRCEDRLaaHDALGGAAKDPKL---LERVKAIREELTNLS----------------------------KPL 2933
Cdd:TIGR00606  613 ELESKEEQLSSYEDKL--FDVCGSQDEESDLerlKEEIEKSSKQRAMLAgatavysqfitqltdenqsccpvcqrvfQTE 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2934 QSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEK- 3012
Cdd:TIGR00606  691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEq 770
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3013 ---LSPPGREIKIVQVQIDDVGKIQtkldRLVGRLEDAERAADVLVDAGFAADTTQTREQIstlrktlgRLDNRVRDHE- 3088
Cdd:TIGR00606  771 etlLGTIMPEEESAKVCLTDVTIME----RFQMELKDVERKIAQQAAKLQGSDLDRTVQQV--------NQEKQEKQHEl 838
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3089 DNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDfrnfrerKVEPLAINVDKVNVAGRDlvrsa 3168
Cdd:TIGR00606  839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE-------QLVELSTEVQSLIREIKD----- 906
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3169 gSGVSTTAIEKDLEKLNDRWNDLKERMNERDRrldVALLQSGKFQEALAGLSKWLSDTEEMVANQKppsSDYKvvkaqlq 3248
Cdd:TIGR00606  907 -AKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVKNIHGYMKDIENKIQDGK---DDYL------- 972
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3249 eqkflkkmlLDRQNSMGSLANLGKEVANHcepgerasiEKQLNDLMKRFDALTDGAEQRELDLEEAMEVAKRfHDKISPL 3328
Cdd:TIGR00606  973 ---------KQKETELNTVNAQLEECEKH---------QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR-ENELKEV 1033
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 386767917  3329 ELWLDNTERSVKAMELIPTDEE--KIQQRIREHDRLHDEILGKKPDFSD 3375
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEhqKLEENIDLIKRNHVLALGRQKGYEK 1082
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
3777-4293 8.26e-05

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: 49.66  E-value: 8.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3777 DQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALgalvADDDGAKINEILD-TDNARYAALRLELRERQQALESALQESS 3855
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEEIKKKSENY----IDEIKAQINDLEDvADKAISNDDPEEIEKKIENIVTKIDKKK 1186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3856 QFSDKLEGMLRALANTVDQVNQLDPLSALP------------QKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKA 3923
Cdd:TIGR01612 1187 NIYDEIKKLLNEIAEIEKDKTSLEEVKGINlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM 1266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3924 GNKADpavrdIKAKLEKLN---NLWNDVQNATKKRGSSLDDI----LSVAEPFWKQ--LNSVMKTLKdlEETLSCQEPPA 3994
Cdd:TIGR01612 1267 GIEMD-----IKAEMETFNishDDDKDHHIISKKHDENISDIreksLKIIEDFSEEsdINDIKKELQ--KNLLDAQKHNS 1339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3995 AQPQDIKK-----QQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMCGEPDK-----------PEVKKHIE------DLDN 4052
Cdd:TIGR01612 1340 DINLYLNEianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKlikkikddinlEECKSKIEstlddkDIDE 1419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4053 AWDNITAL--YAKREENLIDAMEK-AMEFHETLQNLLKFLTKAEDKFAHLGAVGSD---------IDAVKRQIEQLKSFK 4120
Cdd:TIGR01612 1420 CIKKIKELknHILSEESNIDTYFKnADENNENVLLLFKNIEMADNKSQHILKIKKDnatndhdfnINELKEHIDKSKGCK 1499
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4121 DEVDPHMVEVEALNRGLKRQAVELTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLehaLLHLGQFQHALNEllv 4200
Cdd:TIGR01612 1500 DEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKF---ILEAEKSEQKIKE--- 1573
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4201 wINKTDSTLD----------------QLKPIPGDPQLLEVELAKLKVlaNDIQAHQNSVD----TLNdAGRQLIETEKGS 4260
Cdd:TIGR01612 1574 -IKKEKFRIEddaakndksnkaaidiQLSLENFENKFLKISDIKKKI--NDCLKETESIEkkisSFS-IDSQDTELKENG 1649
                          570       580       590
                   ....*....|....*....|....*....|...
gi 386767917  4261 VEASTTQEKLRKLNNEWKQLlqkaSDRQHELEE 4293
Cdd:TIGR01612 1650 DNLNSLQEFLESLKDQKKNI----EDKKKELDE 1678
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4304-4403 9.73e-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: 44.62  E-value: 9.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4304 EVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIKRQnqmKVSSSNLQHTLRT 4383
Cdd:pfam00435    9 DADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG---HYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|
gi 386767917  4384 LKQRWDAVVSRASDKKIKLE 4403
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLE 104
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
227-322 1.07e-04

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 44.22  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  227 ALLRWARRSTaryPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHiVEKEYGVTRLLDPEDVD 306
Cdd:cd21185     5 ATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
                          90
                  ....*....|....*.
gi 386767917  307 TNEPDEKSLITYISSL 322
Cdd:cd21185    81 DPEVEHLGIMAYAAQL 96
SPEC smart00150
Spectrin repeats;
594-688 1.44e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917    594 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 670
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVeaLNELGEQLIEEGHPDAEEiEERLEELN 83
                            90
                    ....*....|....*...
gi 386767917    671 KVYAELLSTSTKRLSDLD 688
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
5055-5116 1.63e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 5055 LTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5116
Cdd:COG5126    35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
PRK01156 PRK01156
chromosome segregation protein; Provisional
3888-4441 1.70e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.36  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3888 IREQIEDNDALMDDLDKRQDAFSAVQRAANDVIakagNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAE 3967
Cdd:PRK01156  202 IKKQIADDEKSHSITLKEIERLSIEYNNAMDDY----NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3968 -----------PFWKQLNSV------MKTLKDLEETLSCQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSN 4030
Cdd:PRK01156  278 leerhmkiindPVYKNRNYIndyfkyKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4031 LmnmcgepdkpevKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLQnlLKFLTKAEDKfAHLGAVGSDIDAVK 4110
Cdd:PRK01156  358 L------------EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK--IQEIDPDAIK-KELNEINVKLQDIS 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4111 RQIEQLKSFKDEVDPHMVEVEALNRGLKRQAVELTERTS--PEQAASIREPLSVVNRRWEALLRGMVERQKQLEHALLHL 4188
Cdd:PRK01156  423 SKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4189 GQFQHAL-----NELLVWINKTDSTLDQLKPIPGDpqllEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIETEKGSVEA 4263
Cdd:PRK01156  503 KKRKEYLeseeiNKSINEYNKIESARADLEDIKIK----INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS 578
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4264 STTQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEvqdilgWLGDVDavigaskpvgglpetatEQLERFMEVY 4343
Cdd:PRK01156  579 LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK------SIREIE-----------------NEANNLNNKY 635
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4344 NELDENRPKVETIQ----------AQGQEYIKRQNQMKVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFH 4413
Cdd:PRK01156  636 NEIQENKILIEKLRgkidnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
                         570       580
                  ....*....|....*....|....*...
gi 386767917 4414 DTLQAFVEWLTQAEKLLSNAEPVSRVLE 4441
Cdd:PRK01156  716 DRINDINETLESMKKIKKAIGDLKRLRE 743
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
3808-3954 1.76e-04

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 46.64  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3808 EALGALVADDDGAKiNEILDtdnaRYAALRLELRERQQALESALQESSQFSDKLEGMLRALANTVDQVN-QLDPLSALPQ 3886
Cdd:cd21116    80 ELADNLIKGDQGAK-QQLLQ----GLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQaQVAVLNALKN 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767917 3887 KIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRD-IKAKLEKLNNLWNDVQNATKK 3954
Cdd:cd21116   155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAfLQADLKAAKADWNQLYEQAKS 223
SPEC smart00150
Spectrin repeats;
3537-3628 1.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   3537 QQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIESIV 3607
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAsedlGKDLESVEALlkkheAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 386767917   3608 TRDNRRFDSIVEQIQRKAERL 3628
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1712-1957 2.07e-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: 45.90  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1712 ELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKFVDESKEflailnd 1791
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1792 frtslperlphveplssAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDkANEWLRSvhpRVSRIIS 1871
Cdd:cd00176    73 -----------------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEE---KEAALAS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1872 EPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSlggqLSPMEINQLELPIADLKNNYQQLLDNLGEHCK 1951
Cdd:cd00176   132 EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQK 207

                  ....*.
gi 386767917 1952 TLDKTL 1957
Cdd:cd00176   208 KLEEAL 213
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
223-322 2.08e-04

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409161  Cd Length: 114  Bit Score: 44.03  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  223 SAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 301
Cdd:cd21312    12 TPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 88
                          90       100
                  ....*....|....*....|.
gi 386767917  302 PEDVDTNEPDEKSLITYISSL 322
Cdd:cd21312    89 PEEIVDPNVDEHSVMTYLSQF 109
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3281-4026 2.14e-04

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: 48.14  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3281 GERASIEKQLNDLMKRFDALTDGAEQRELDLEEA--------MEVAKRFHDKISPLELWLDNTERSVKAMELIPTD-EEK 3351
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDaEER 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3352 IQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAVnLGEKVRGVTErytglVDASdnigalLAESRQGLRHLV 3431
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEE-----VDKE------FAETRDELKDYR 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3432 LSYQDLVAWMESMEAELKRFKsvpvyaEKLLEQMDHLLELNENIAGHASNVESTVESGAELMKHISNDE--AIQLKDKLD 3509
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQ------EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkLEQLAADLS 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3510 SLQRRYGDLTNRGGDLLKsaqnalplvqQFHEAHNRLVEwmqsAEAALAPSEPRQADVLRLEGEL-ADMRPILDSINQ-- 3586
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEK----------ELSKLQRELAE----AEAQARASEERVRGGRAVEEVLkASIQGVHGTVAQlg 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3587 -VGPQLCQLSPGEGAATIESIVTRDNrrfDSIVEQIQ----RKAER---LHLSNQRAKEVTGDIdellewfREMDTTLRE 3658
Cdd:TIGR02169  532 sVGERYATAIEVAAGNRLNNVVVEDD---AVAKEAIEllkrRKAGRatfLPLNKMRDERRDLSI-------LSEDGVIGF 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3659 A-DLPAMEPKLVRAQLQEHRS--INDDISSQK---GRVRDVT-----------------AASKKVLRESPQSENTATLRE 3715
Cdd:TIGR02169  602 AvDLVEFDPKYEPAFKYVFGDtlVVEDIEAARrlmGKYRMVTlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3716 KLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDMEQQISRLS--MPALRPDQITLQQ---DKNERLL 3790
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLEQeieNVKSELK 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3791 QSIAEHKPLLDKLNKTGEALGALVADDDGAKINEI---LDTDNARYAALRLELRERQQALESALQESSQFSDKLEGMLRA 3867
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3868 LANTVDQVN----QLDPLSALPQKIREQIEDNDALMDDLDKRqdaFSAVQRAANDVIAKaGNKADPAVRDIKAKLEKLnn 3943
Cdd:TIGR02169  842 RIDLKEQIKsiekEIENLNGKKEELEEELEELEAALRDLESR---LGDLKKERDELEAQ-LRELERKIEELEAQIEKK-- 915
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3944 lwNDVQNATKKRGSSLDDILSVAEPFWKQ----------LNSVMKTLKDLEETLSCQEP-----------PAAQPQDIKK 4002
Cdd:TIGR02169  916 --RKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPvnmlaiqeyeeVLKRLDELKE 993
                          810       820
                   ....*....|....*....|....
gi 386767917  4003 QQVALQEIRHEIDQTKPEVEQVRR 4026
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKR 1017
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2843-3100 2.39e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2843 DKEPIKAELQDIRDRWERLNndliaRAHE-IENCSRRLDDFnDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKA 2921
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLE-----RAHEaLEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2922 IREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGL-ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 3000
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3001 IDLNDLETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLVDAgFAADTTQTREQISTLRKTLGRL 3080
Cdd:COG4913   373 LPLPASAEEFAAL--------------------RAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASL 431
                         250       260
                  ....*....|....*....|
gi 386767917 3081 DNRVRDHEDNLHSTLKALRE 3100
Cdd:COG4913   432 ERRKSNIPARLLALRDALAE 451
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
885-922 2.44e-04

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386767917  885 KQQGQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIP 922
Cdd:cd11768    11 IEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIP 48
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2847-3013 2.86e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2847 IKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALggAAKDPKLLERVKAIREeL 2926
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--IKKYEEQLGNVRNNKE-Y 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2927 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAatavsqfneqmkslgidLNDL 3006
Cdd:COG1579    92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE-----------------LAEL 154

                  ....*..
gi 386767917 3007 ETEIEKL 3013
Cdd:COG1579   155 EAELEEL 161
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1607-1782 3.04e-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: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1607 VNDLLKWVTTVEQKISSvGGPREKIDELRNQINALKQIKDEIESQQRPVATCLEQIRQIVLTGgdvlsAPEVTTLENSGR 1686
Cdd:cd00176     9 ADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1687 ELRSRVDRVNDRTVRLLRRLEAGRDELTKLRsELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQA 1766
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHEP 160
                         170
                  ....*....|....*.
gi 386767917 1767 DLRFITMAAQKFVDES 1782
Cdd:cd00176   161 RLKSLNELAEELLEEG 176
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
376-567 3.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  376 EMKRLLSDLQRFRSDEVSARKREK------------SKLIQIYKELERYFETVGEVDVEaELRPDA--IEKAWYRMNTaL 441
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLE-ELEKKAeeYEKLKEKLIK-L 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  442 QDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEG--------RRIERLHP--------VDAKSIVEAL 505
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleERLKELEPfyneylelKDAEKELERE 617
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917  506 ETEIRHLEEPIQDMNQDCHVLNEgrypHVSELHKKVNKLHQRWAQLR----TNFHTNLVQKLSGLK 567
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEK----RLEELRKELEELEKKYSEEEyeelREEYLELSRELAGLR 679
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5225-5442 3.78e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5225 TPRRSTPNAAATASSSPHAHNGGSSNLPPYMS------GQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSlsdnegSHG 5298
Cdd:PHA03307  112 SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSpgpppaASPPAAGASPAAVASDAASSRQAALPLSSPEET------ARA 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5299 GPSGRYTPRkvtyTSTRTGLTPGGSRAGSKPNSRPLSRQGSKPPsRHGSTLSLDSTDDHTPSRipqrKPSTGSTASGTTP 5378
Cdd:PHA03307  186 PSSPPAEPP----PSTPPAAASPRPPRRSSPISASASSPAPAPG-RSAADDAGASSSDSSSSE----SSGCGWGPENECP 256
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767917 5379 RParlSVTTTTTPGSRLNGTSTITRKTASGSASPAPTRRNISGSSTPSgmqTPRKSSAEPTFSS 5442
Cdd:PHA03307  257 LP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS---SPGSGPAPSSPRA 314
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4102-4182 4.06e-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: 42.69  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4102 VGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRglkrQAVELTERtSPEQAASIREPLSVVNRRWEALLRGMVERQKQL 4181
Cdd:pfam00435   29 YGKDLESVQALLKKHKALEAELAAHQDRVEALNE----LAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKL 103

                   .
gi 386767917  4182 E 4182
Cdd:pfam00435  104 E 104
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5225-5393 4.15e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5225 TPR-RSTPNAAATASSSPHAHNGGSSnLPPYMSGQGPIikvRERS---------VRSIPMSRPSRSSLSASTPDSLSDNE 5294
Cdd:PHA03307  255 CPLpRPAPITLPTRIWEASGWNGPSS-RPGPASSSSSP---RERSpspspsspgSGPAPSSPRASSSSSSSRESSSSSTS 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 5295 GSHGGPSGRYTPRKVTYTSTRTGLTPGGSRAGSKPNSRPLSRQGSKPPSRH--------------GSTLSLDSTDDHTPS 5360
Cdd:PHA03307  331 SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASagrptrrraraavaGRARRRDATGRFPAG 410
                         170       180       190
                  ....*....|....*....|....*....|...
gi 386767917 5361 RIPQRKPSTGSTASGTTPRPARLSVTTTTTPGS 5393
Cdd:PHA03307  411 RPRPSPLDAGAASGAFYARYPLLTPSGEPWPGS 443
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1999-2181 4.37e-04

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 46.71  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1999 IREHKVLLADLQSHQASIDSVQVSAKHLLASASNARI--AKKVESNLNDVtvkfekLYEKANKRGEFLDDVYNRLSRYLD 2076
Cdd:COG5391   303 FSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGvfAKRLEQNQNSI------LNEGVVQAETLRSSLKELLTQLQD 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2077 EISTVEQRMASLQEALDSRETSLLSTEELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQW 2156
Cdd:COG5391   377 EIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDK 456
                         170       180       190
                  ....*....|....*....|....*....|
gi 386767917 2157 RNI----NISIDERAKLSKQ-KAEQQLAYE 2181
Cdd:COG5391   457 EKLeeqlAIAEKDAQEINEElKNELKFFFS 486
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
878-926 4.62e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 40.98  E-value: 4.62e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 386767917    878 VQAICAYKQQ--GQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACL 926
Cdd:smart00326    5 VRALYDYTAQdpDELSFKKGDIITVLEKSDDGWWKGRLGRGKEGLFPSNYV 55
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
3932-4548 6.77e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.50  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3932 RDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQvaLQEIR 4011
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQL--LKQLR 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4012 HEIDQTKPEVeqvrrhgsnlmnmcgepdkPEVKKHIEDLDNAWDniTALYAKREENLIDAMEKAMEFHETLQNLLKFLTK 4091
Cdd:TIGR00618  267 ARIEELRAQE-------------------AVLEETQERINRARK--AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4092 AEDKFAHLGAVGSDIDAVKRQIEQLKSFKDEVdphmvevealnrglkrqavelteRTSPEQAASIREPLsvvnrrweall 4171
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-----------------------RDAHEVATSIREIS----------- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4172 rgmvERQKQLEHALLHLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLAndiqAHQNSVDTLNDAGR 4251
Cdd:TIGR00618  372 ----CQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA-TIDTRTSAFRDLQGQLAH----AKKQQELQQRYAEL 442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4252 QLIETEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQ--HELEEALREAHGYIAEVQDILGWLGDVDAVIGASKPV-GGL 4328
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdIDN 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4329 PETATEQLERFMEVYNELDEnrpKVETIQAQGQEYIKRQNQMKVSSSNLQHTLRTLKQRWDAvVSRASDKKIKLEIALKE 4408
Cdd:TIGR00618  523 PGPLTRRMQRGEQTYAQLET---SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR-SKEDIPNLQNITVRLQD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4409 ATEFHDTLQAFVEWLTQAEKLlsNAEPVSRVLETIQAQMEEHKVLQKDVST-HREAMLLLDKKGTH---LKYFSQKQDVI 4484
Cdd:TIGR00618  599 LTEKLSEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLTLTQERVREhalSIRVLPKELLA 676
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767917  4485 LIKNLLVSVQHRWERVV----------SKAAERTRALDHGYKEAREFNDAWSGMMQYLQETEQVLDQIIEEATA 4548
Cdd:TIGR00618  677 SRQLALQKMQSEKEQLTywkemlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2344-2552 7.35e-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: 44.36  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2344 ELRKQYENLKGLAQFLERIQRQLPKESVSNK-DEAERCIKQARKILEDMYEKQSLLDTTKAQVKDILRrkSDVPGAEQLR 2422
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDlESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2423 QENDSIQEKWKNLNDICKNR---IAFSEKLRDFLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRT 2499
Cdd:cd00176    79 ERLEELNQRWEELRELAEERrqrLEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386767917 2500 QQPQLKHFQELGHDVVDHlAGTPDAQAVEIKLKDILGKWDDLVGKLDDRANSL 2552
Cdd:cd00176   158 HEPRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1012-1857 8.04e-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: 46.20  E-value: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1012 QLRRLRREMDEVNRLFDEFEKRARAEEesKQASRifTEECLAIKSKLedmaRELDQIILAPLPRDL-DSLEHVLEIHSDY 1090
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELERQLKSLE--RQAEK--AERYKELKAEL----RELELALLVLRLEELrEELEELQEELKEA 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1091 ERRLHLLEPELKHLQETFRTIALKTPVLKKSLDNLMELWKEL-NTQSGLHKdRLKLLEASLAGLEDNehvISELENELAR 1169
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaNEISRLEQ-QKQILRERLANLERQ---LEELEAQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1170 HQdlpstaEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLgrmgvpTKVLGDLKRLHSNVERLNTRWSAVCNQLGERM 1249
Cdd:TIGR02168  328 LE------SKLDELAEELAELEEKLEELKEELESLEAELEEL------EAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1250 RSCETAIGLMKNLQSSVQVEeswVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENVNVAGGRLIREAKIYDskclr 1329
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDR---RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR----- 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1330 fvDWLVEARPSFSPPRRDLRPADSDPGATQYYSQRLDNLN------TKN--------DRLLEQLS--QRLKTAIEVNGSD 1393
Cdd:TIGR02168  468 --EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkalLKNqsglsgilGVLSELISvdEGYEAAIEAALGG 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1394 GLQY-----------AESLQKPLKTFRVDFSAGSVPTGDGYAARQEDLYTTtysttqisSTKTTKSSTKSVYSSDGLDAA 1462
Cdd:TIGR02168  546 RLQAvvvenlnaakkAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN--------IEGFLGVAKDLVKFDPKLRKA 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1463 -----SQEVSTAGLPQSQIQFNEIRTLKRSQQLGGHSVLD---IAGIRDPRTGRVLtigeAIQLRILDVRTgemlvgdRR 1534
Cdd:TIGR02168  618 lsyllGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSIL----ERRREIEELEE-------KI 686
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1535 ITLEQAADQGLIDLQLAKQLLEpgAGRDASGRELSLLEVIQREISEAESGYETAEKRIKQavfekfnmCEENVNDLLKWV 1614
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKEL 756
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1615 TTVEQKISSVGGPREKIDElrnqinALKQIKDEIESQQRPVATCLEQIrqivltggdvlsapevTTLENSGRELRSRVDR 1694
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEE------ELAEAEAEIEELEAQIEQLKEEL----------------KALREALDELRAELTL 814
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1695 VNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVREFVSDVI-GHQADLRFITM 1773
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERaSLEEALALLRS 894
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1774 AAQKFVDESKEFLAILNDFRTSLPERlphveplssaespiRQEVSLVSAQYKDLLNRVNALQDRVSGLGgrQREYQDALD 1853
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEEL--------------REKLAQLELRLEGLEVRIDNLQERLSEEY--SLTLEEAEA 958

                   ....
gi 386767917  1854 KANE 1857
Cdd:TIGR02168  959 LENK 962
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1566-2078 9.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 9.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1566 RELSLLEVIQREISEAESGYETAEKRIKqAVFEKFNMCEENVNDLLKWVTTVEQKIssvGGPREKIDELRNQINALKQIK 1645
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1646 DEIESQqRPVATCLEQIRQIVLTGGDVLSAPEVT--TLENSGRELRSRVDRVNDRTVRLlRRLEAGRDELTKLRSELDVF 1723
Cdd:PRK03918  283 KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRlsRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1724 SDWLQVARRTLEDKERSLSDLTRLPSQaDSVREfvsdvighqadLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHV 1803
Cdd:PRK03918  361 HELYEEAKAKKEELERLKKRLTGLTPE-KLEKE-----------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1804 EPLSSAES-------PIRQE-----VSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDKAN---------EWLRSV 1862
Cdd:PRK03918  429 EELKKAKGkcpvcgrELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKEL 508
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1863 HPRVSRIISEP-----------------IAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSLGgQLSPMEI 1925
Cdd:PRK03918  509 EEKLKKYNLEElekkaeeyeklkeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1926 NQLELPIADLKNNY-------------QQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIK 1992
Cdd:PRK03918  588 EELEERLKELEPFYneylelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELR 665
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1993 ERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANK-RGEFLDDVYNRL 2071
Cdd:PRK03918  666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKyKALLKERALSKV 745

                  ....*..
gi 386767917 2072 SRYLDEI 2078
Cdd:PRK03918  746 GEIASEI 752
PLEC smart00250
Plectin repeat;
1498-1526 1.02e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 1.02e-03
                            10        20
                    ....*....|....*....|....*....
gi 386767917   1498 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1526
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4138-4458 1.05e-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: 45.83  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4138 KRQAVELTERTSpEQAASIREPLSVVNRRWEALLRgmvERQKQLEHALLHLGQFQHALNELLvwiNKTDSTLDQLKPIPG 4217
Cdd:TIGR02169  172 KEKALEELEEVE-ENIERLDLIIDEKRQQLERLRR---EREKAERYQALLKEKREYEGYELL---KEKEALERQKEAIER 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4218 DPQLLEVELAKLKVLANDIQAHQNS-VDTLNDAGRQLieTEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALR 4296
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEiEQLLEELNKKI--KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4297 EAHGYIAEVQDILGWLGDVDAVIGA-SKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIKRQNQMKVSSS 4375
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  4376 NLQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDTLQAFVEWLTQAE-KLLSNAEPVSRVLETIQAQMEEHKVLQ 4454
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwKLEQLAADLSKYEQELYDLKEEYDRVE 482

                   ....
gi 386767917  4455 KDVS 4458
Cdd:TIGR02169  483 KELS 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-709 1.05e-03

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: 45.82  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   335 LFDMESQ-RRVHEYRDLAQQFiywcREKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYF 413
Cdd:TIGR02168  195 LNELERQlKSLERQAEKAERY----KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   414 ETVGEVdVEAELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLegrigeegrrierl 493
Cdd:TIGR02168  271 ELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------------- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   494 hpvdaKSIVEALETEIRHLEEPIQDMNQDchvlnegryphVSELHKKVNKLHQRWAQLRTNfHTNLVQKLSGLKypvHET 573
Cdd:TIGR02168  336 -----AEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQ-LETLRSKVAQLE---LQI 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   574 TVTRQTRMVVESRQIDTNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEhkiidqfhtkiLNDERQQTK 653
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE-----------LERLEEALE 464
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917   654 FSGDELALYQQRLNQLQKVYAELLStstkRLSDLDSLQ-HFLGQASAELQWLNEKEQ 709
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQA----RLDSLERLQeNLEGFSEGVKALLKNQSG 517
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2847-3367 1.19e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2847 IKAELQDIRDRWERLNNdliarahEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAhdalggaakdpkLLERVKAIREEL 2926
Cdd:COG1196   258 LEAELAELEAELEELRL-------ELEELELELEEAQAEEYELLAELARLEQDIAR------------LEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2927 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDL 3006
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3007 ETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLvdagfAADTTQTREQISTLRKTLGRLDNRVRD 3086
Cdd:COG1196   399 AAQLEEL--------------------EEAEEALLERLERLEEELEEL-----EEALAELEEEEEEEEEALEEAAEEEAE 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3087 HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDF--------RNFRERKVEPLAINVDKVN 3158
Cdd:COG1196   454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalLLAGLRGLAGAVAVLIGVE 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3159 VAGRDLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDTEEMVANQKPPSS 3238
Cdd:COG1196   534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3239 DYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAMEVA 3318
Cdd:COG1196   614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386767917 3319 KRFHDKISPLELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEIL 3367
Cdd:COG1196   694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3755-3848 1.27e-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: 41.54  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3755 LTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALVaDDDGAKINEILDTDNARYA 3834
Cdd:pfam00435   13 LESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERLEELNERWE 90
                           90
                   ....*....|....
gi 386767917  3835 ALRLELRERQQALE 3848
Cdd:pfam00435   91 QLLELAAERKQKLE 104
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2545-3118 1.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2545 LDDRANSLGG-----AADSSKEFDAAVNRLREALQNISDNLDTLPTDGDHQENLRkiENLERQLEGQRPLLADVEQSAAT 2619
Cdd:PRK02224  182 LSDQRGSLDQlkaqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVLEEHEERREELETLEAE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2620 LcnilgdpasrADVNSRVAALEKQYLALQKKLDTKKAETEASLRDGRHFAENCsktlgwlggELSNLtDRLLVSAHKPTL 2699
Cdd:PRK02224  260 I----------EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA---------GLDDA-DAEAVEARREEL 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2700 QHQIDTHEPIYREVMAREHEVimlinkgkdltdRQQDRGVKRDLDRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSE 2779
Cdd:PRK02224  320 EDRDEELRDRLEECRVAAQAH------------NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2780 TFLAWLRTAEDKLADLTpgvLSKAKLETRLRDLQTFRSEVWKHSGEFEntkglgetflsscdidkepikAELQDIRDRWE 2859
Cdd:PRK02224  388 ELEEEIEELRERFGDAP---VDLGNAEDFLEELREERDELREREAELE---------------------ATLRTARERVE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2860 RlNNDLIA---------------RAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKD-PKLLERVKAI- 2922
Cdd:PRK02224  444 E-AEALLEagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRiERLEERREDLe 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2923 ------REELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQF---- 2992
Cdd:PRK02224  523 eliaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaia 602
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2993 ---------NEQMKSLGiDLNDLETeiEKLSPPGREIKIVQVQIDDvgkiqtklDRLVGRLEDAERAADVLVDAgfAADT 3063
Cdd:PRK02224  603 daedeierlREKREALA-ELNDERR--ERLAEKRERKRELEAEFDE--------ARIEEAREDKERAEEYLEQV--EEKL 669
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386767917 3064 TQTREQISTLRKTLGRLDNRVRDhednlhstLKALREFYDHQSQTLDDIQDVSDE 3118
Cdd:PRK02224  670 DELREERDDLQAEIGAVENELEE--------LEELRERREALENRVEALEALYDE 716
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
993-1150 1.37e-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: 43.59  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  993 RALNDDADKLLSEGDPNDPQLRRlrrEMDEVNRLFDEFEKRARAEEESKQASRI---FTEECLAIKSKLEDMARELDQIi 1069
Cdd:cd00176    57 EALNELGEQLIEEGHPDAEEIQE---RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASE- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1070 laPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTI-----ALKTPVLKKSLDNLMELWKELNTQSglhKDRLK 1144
Cdd:cd00176   133 --DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELleeghPDADEEIEEKLEELNERWEELLELA---EERQK 207

                  ....*.
gi 386767917 1145 LLEASL 1150
Cdd:cd00176   208 KLEEAL 213
SPEC smart00150
Spectrin repeats;
1153-1253 1.38e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.16  E-value: 1.38e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   1153 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1232
Cdd:smart00150    7 ADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 386767917   1233 RLNTRWSAVCNQLGERMRSCE 1253
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3674-3942 1.41e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3674 QEHRSINDDISSQKGRVRDVTAASKKVLRESPQSENTATLREKLDDLKEIVDTVAQLcSERLGILEQALPLSEHFADSHQ 3753
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3754 GLTAWLDDMEQQISRLSmpalrpDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEAlgALVADDDGAKINEILDtdnARY 3833
Cdd:COG4913   696 ELEAELEELEEELDELK------GEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGD---AVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3834 AALRLELRERQQALESALQESSQfsdKLEGMLRALANT-VDQVNQLDP-LSALP--QKIREQIEDndalmDDL-DKRQDA 3908
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEE---ELERAMRAFNREwPAETADLDAdLESLPeyLALLDRLEE-----DGLpEYEERF 836
                         250       260       270
                  ....*....|....*....|....*....|....
gi 386767917 3909 FSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLN 3942
Cdd:COG4913   837 KELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-1213 1.50e-03

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: 45.43  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   436 RMNTALQDREVILQqEIER-LERLQRLADKVQR------EIKHVDqkLTDLEGRIGEEGRRIERLhpvdaKSIVEALETE 508
Cdd:TIGR02168  183 RTRENLDRLEDILN-ELERqLKSLERQAEKAERykelkaELRELE--LALLVLRLEELREELEEL-----QEELKEAEEE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   509 IRHLEEPIQDMNQDchvlnegryphVSELHKKVNKLHQRWAQLRTNFHtNLVQKLSGLKypvHETTVTRQTRMVVESRQI 588
Cdd:TIGR02168  255 LEELTAELQELEEK-----------LEELRLEVSELEEEIEELQKELY-ALANEISRLE---QQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   589 DTNPHFRDLQEHIEwCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKILNDERQQTKFSGDELALYQQ-RLN 667
Cdd:TIGR02168  320 ELEAQLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   668 QLQKVYAEllststkrlSDLDSLQHFLGQASAELQWLNEKEQveitrdwadkQLDLPSVHRYYENLMSELEKREMHfati 747
Cdd:TIGR02168  399 NNEIERLE---------ARLERLEDRRERLQQEIEELLKKLE----------EAELKELQAELEELEEELEELQEE---- 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   748 LDRGEALLNQQHPASKCIEAHLTALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSqSDFG 827
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEG 534
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   828 LDQG-ETLLRG-MQDL-REELNAFGETVATL-QRRAQTVVPLnkrrqpvnrqgPVQAICAYKQQG-QLQIEKGETVTLLD 902
Cdd:TIGR02168  535 YEAAiEAALGGrLQAVvVENLNAAKKAIAFLkQNELGRVTFL-----------PLDSIKGTEIQGnDREILKNIEGFLGV 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   903 NSGRVKWRVRtAKGQEGPIPGACLLLPPPDQeaidAAERLKRLFDRSVALWQKKHL-----------RLRQNMIFATIRV 971
Cdd:TIGR02168  604 AKDLVKFDPK-LRKALSYLLGGVLVVDDLDN----ALELAKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRRE 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   972 VKgwDFDQFLAMGPEQRTAIRRALNdDADKLLSEGdpnDPQLRRLRREMDEVNRLFDEFEKR-ARAEEESKQASRIFTEE 1050
Cdd:TIGR02168  679 IE--ELEEKIEELEEKIAELEKALA-ELRKELEEL---EEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQL 752
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1051 CLAIKSKLEDMARELDQII-----LAPLPRDLDSLEHVLEihsDYERRLHLLEPELKHLQETFRTialktpvLKKSLDNL 1125
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEeaeeeLAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTL-------LNEEAANL 822
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1126 MELWKELNTQSGLHKDRLKLLEASlagLEDNEHVISELENELARHQDLPSTAEglqqvfKQLNHMQDIITQQQPQMDKMN 1205
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELE------SELEALLNERASLEEALALLR 893

                   ....*...
gi 386767917  1206 DAADQLGR 1213
Cdd:TIGR02168  894 SELEELSE 901
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1628-2463 1.51e-03

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: 45.42  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1628 REKIDELRNQINALKQIKDEIESQQRPvatcLEQIRQIVLTGGDvlsaPEVTTL-ENSGRELRSRVDRVNDrTVRLLRRL 1706
Cdd:TIGR00606  261 LSKIMKLDNEIKALKSRKKQMEKDNSE----LELKMEKVFQGTD----EQLNDLyHNHQRTVREKERELVD-CQRELEKL 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1707 EAGRDELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADS-VREFVSDVIGHQADLRFITMAAQKFVDESKEF 1785
Cdd:TIGR00606  332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-RDSLIQSLATRLeLDGFERGPFSERQIKNFHTLVIERQEDEAKTA 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1786 LAILNDFRTSLPERlphveplSSAESPIRQEVSLVSaqyKDLLNRVNALQDRVSGLGGRQREYQDALDKANEWLRSVHPR 1865
Cdd:TIGR00606  411 AQLCADLQSKERLK-------QEQADEIRDEKKGLG---RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1866 VSRIISEPIAGDPKGVQDQMNEAKALHNE---LLSSGRLVDNAQQALDNLLRSLggqlspmeiNQLELPIADLKNNYQQL 1942
Cdd:TIGR00606  481 RKAERELSKAEKNSLTETLKKEVKSLQNEkadLDRKLRKLDQEMEQLNHHTTTR---------TQMEMLTKDKMDKDEQI 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1943 LDNLGEHCKTLDKTL---VQSQGVQDALDSLVGWVNQAEDKF-KMNLRPASLikERLQEQIR-EHKVLLADLQSHQASID 2017
Cdd:TIGR00606  552 RKIKSRHSDELTSLLgyfPNKKQLEDWLHSKSKEINQTRDRLaKLNKELASL--EQNKNHINnELESKEEQLSSYEDKLF 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2018 SVQVSakhllasasnariaKKVESNLNdvtvKFEKLYEKANKRGEFLDDVYNRLSRYLDEIST-----------VEQRMA 2086
Cdd:TIGR00606  630 DVCGS--------------QDEESDLE----RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrVFQTEA 691
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2087 SLQEALDSRETSLLST----EELARRMNELSRDKDQLAPQFEdcvrsGKDLISLRDVTDTGVLRDRIKALESQWRNINIS 2162
Cdd:TIGR00606  692 ELQEFISDLQSKLRLApdklKSTESELKKKEKRRDEMLGLAP-----GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2163 IDERAK-LSKQKAEQQLAYEGLKDQVLswlastearvnglppvaidldrIKQQHDELKPICKDYRDYAPTIDKInDIGAQ 2241
Cdd:TIGR00606  767 IEEQETlLGTIMPEEESAKVCLTDVTI----------------------MERFQMELKDVERKIAQQAAKLQGS-DLDRT 823
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2242 YDALiRPESPARKRSTYSPIKRTSPLRRMSGDARSPSPTKGGILSPLSTGSsgfgsrrssqdgFQLSELSPVQQQLSEin 2321
Cdd:TIGR00606  824 VQQV-NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK------------LQIGTNLQRRQQFEE-- 888
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2322 nrygligvRLNDRQHELDNLNEELRKQYENLKGLAQFLERIQRQlpKESVSNKDEAERciKQARKILEDMYEKqslLDTT 2401
Cdd:TIGR00606  889 --------QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISSKETSN--KKAQDKVNDIKEK---VKNI 953
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917  2402 KAQVKDILRRKSDvpGAE-QLRQENDSIQEKWKNLNDICKNRIAFSEKLRDF---LDTHGNLKSWL 2463
Cdd:TIGR00606  954 HGYMKDIENKIQD--GKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMrqdIDTQKIQERWL 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1666-2065 1.63e-03

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: 45.05  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1666 VLTGGDVLSAPEVTTLENSGRELRSRVDRvndrtvrLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLt 1745
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL- 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1746 rlpsqadsvrefvsdvighQADLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHVEPLSSAESPIRQEVSLVSAQYK 1825
Cdd:TIGR02168  732 -------------------RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1826 DLLNRVNALQDRVSGLGGRQREYQDALDKANEWLRSVHPRVSRIISEpiAGDPKGVQDQMNE-AKALHNELLSSGRLVDN 1904
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR--LEDLEEQIEELSEdIESLAAEIEELEELIEE 870
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1905 AQQALDNLLRslggqlspmEINQLELPIADLKNNYQQLLDNLGEhcktLDKTLVQSQGVQDALDSLVGWVNQAEDKFKMN 1984
Cdd:TIGR02168  871 LESELEALLN---------ERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELREKLAQLELRLEGLEVR 937
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1985 LrpaslikERLQEQIRE-HKVLLADLQSHQASIDSVQVSAKHLLASASNARiakkveSNLNDVTVKFEKLYEKANKRGEF 2063
Cdd:TIGR02168  938 I-------DNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKI------KELGPVNLAAIEEYEELKERYDF 1004

                   ..
gi 386767917  2064 LD 2065
Cdd:TIGR02168 1005 LT 1006
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
221-324 1.67e-03

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 41.52  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  221 NVSAREALLRW-----ARRSTARYpgvRVNDFTSSWRDGLAFSALVHRNRP---DLLDWRKARNdrPRERLETAFHIVE- 291
Cdd:cd21218     8 YLPPEEILLRWvnyhlKKAGPTKK---RVTNFSSDLKDGEVYALLLHSLAPelcDKELVLEVLS--EEDLEKRAEKVLQa 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 386767917  292 -KEYGVTRLLDPEDVdtNEPDEKSLITYISSLYD 324
Cdd:cd21218    83 aEKLGCKYFLTPEDI--VSGNPRLNLAFVATLFN 114
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
986-1169 1.68e-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: 45.06  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   986 EQRTAIRRALNDDA--DKLLSEGDPNDPQLRRLRRE----MDEVNRLFDEFEK-RARAEEESKQASRIFtEECLAIKSKL 1058
Cdd:TIGR02169  316 ELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDlRAELEEVDKEFAETR-DELKDYREKL 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1059 EDMARELDQIIlAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALKtpvLKKSLDNLMELWKELNTQsgl 1138
Cdd:TIGR02169  395 EKLKREINELK-RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSKY--- 467
                          170       180       190
                   ....*....|....*....|....*....|.
gi 386767917  1139 hKDRLKLLEASLAGLEDNehvISELENELAR 1169
Cdd:TIGR02169  468 -EQELYDLKEEYDRVEKE---LSKLQRELAE 494
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3320-3414 1.70e-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: 41.15  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3320 RFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKV 3399
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERL 82
                           90
                   ....*....|....*
gi 386767917  3400 RGVTERYTGLVDASD 3414
Cdd:pfam00435   83 EELNERWEQLLELAA 97
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2847-2991 2.14e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2847 IKAELQDIRDRWERLNNdliarahEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLErvkAIREEL 2926
Cdd:COG1579    29 LPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE---ALQKEI 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767917 2927 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQ 2991
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
2563-3168 2.20e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2563 DAAVNRLREALQNISDNL-----DTLPTDGDHQENLRKI----ENLERQLEGQRPLLADVEQSAATLCNILGDPASR--A 2631
Cdd:pfam12128  314 DAAVAKDRSELEALEDQHgafldADIETAAADQEQLPSWqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiA 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2632 DVNSRV-----------AALEKQYLALQKKLdtkKAETEASLRDGRHFAENCSKTLGWLGGELSNLTdrllvsAHKPTLQ 2700
Cdd:pfam12128  394 GIKDKLakireardrqlAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT------ATPELLL 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2701 HQIDTHEPIYRevmAREHevimLINKGKDLTDRQQDRGVKRDldRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSET 2780
Cdd:pfam12128  465 QLENFDERIER---AREE----QEAANAEVERLQSELRQARK--RRDQASEALRQASRRLEERQSALDELELQLFPQAGT 535
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2781 FLAWLRTAEDKLADLTPGVLSKAKLetrLR-DLQtfrSEVWKHSGEFENTKGLGETFLSSCDIDK-----EPIKAE---- 2850
Cdd:pfam12128  536 LLHFLRKEAPDWEQSIGKVISPELL---HRtDLD---PEVWDGSVGGELNLYGVKLDLKRIDVPEwaaseEELRERldka 609
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2851 ---LQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGR-----------CEDRLAAHDALGGaakdpkll 2916
Cdd:pfam12128  610 eeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdekqsekdkKNKALAERKDSAN-------- 681
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2917 ERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDAdhlTSEVDGlaDRMSELqGRLDDRCGELQSAATA-VSQFNEQ 2995
Cdd:pfam12128  682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY---WQVVEG--ALDAQL-ALLKAAIAARRSGAKAeLKALETW 755
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2996 MKSlgiDLNDLETEIEKLSPPGREIKIVQVQIDDVGKIQTKldrlVGRLEDAERAADVLVDAGFAADTTQTREQISTLRK 3075
Cdd:pfam12128  756 YKR---DLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  3076 TLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTL---DDIQDVSDEFKRMKPVGS---ELDQIRRQQEDFRNFRERKVEP 3149
Cdd:pfam12128  829 QLARLIADTKLRRAKLEMERKASEKQQVRLSENLrglRCEMSKLATLKEDANSEQaqgSIGERLAQLEDLKLKRDYLSES 908
                          650
                   ....*....|....*....
gi 386767917  3150 LAINVDKVNVAGRDLVRSA 3168
Cdd:pfam12128  909 VKKYVEHFKNVIADHSGSG 927
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
4214-4434 3.36e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4214 PIPGDPQL--LEVELAKLKVLANDIQAHQNSVDT-LNDAGRQLIETEKgsvEASTTQEKLRKLNNEWKQLLQKASDRQHE 4290
Cdd:COG3883    11 PAFADPQIqaKQKELSELQAELEAAQAELDALQAeLEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 4291 LEEALREAhgYIAEvqdilGWLGDVDAVIGAskpvgglpETATEQLERFMevyneldenrpKVETIQAQGQEYIKRQNQM 4370
Cdd:COG3883    88 LGERARAL--YRSG-----GSVSYLDVLLGS--------ESFSDFLDRLS-----------ALSKIADADADLLEELKAD 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767917 4371 KVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDTLQAFVEWLTQAEKLLSNAE 4434
Cdd:COG3883   142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
PRK01156 PRK01156
chromosome segregation protein; Provisional
2735-3203 3.93e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2735 QDRGVKRDLDRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRDL-- 2812
Cdd:PRK01156  208 DDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIin 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2813 ------QTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIK--AELQDIRDRWERLNNDLIARAHEIENCSRRLDDFND 2884
Cdd:PRK01156  288 dpvyknRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2885 ELRNLDHSLGRCED------RLAAH--DALGGAAKDPkllERVKAIREE-----------LTNLSKPLQSLKALAKDISA 2945
Cdd:PRK01156  368 YLKSIESLKKKIEEysknieRMSAFisEILKIQEIDP---DAIKKELNEinvklqdisskVSSLNQRIRALRENLDELSR 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2946 EARAAGGD------ADHLTSE-VDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSL-----GIDLNDLETEIEKL 3013
Cdd:PRK01156  445 NMEMLNGQsvcpvcGTTLGEEkSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeyleSEEINKSINEYNKI 524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3014 SPPGREIKIVQVQIDDVGKIQTKLDRLVGR-----LEDAERAADVLVDAGFAADTTQtreqISTLRKTLGRLDNRVRDHE 3088
Cdd:PRK01156  525 ESARADLEDIKIKINELKDKHDKYEEIKNRykslkLEDLDSKRTSWLNALAVISLID----IETNRSRSNEIKKQLNDLE 600
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3089 DNLHSTLKalrEFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFR----NFRERKVEPLAINVDKVNVAGR-- 3162
Cdd:PRK01156  601 SRLQEIEI---GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRgkidNYKKQIAEIDSIIPDLKEITSRin 677
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386767917 3163 ----DLVRSAG----SGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLD 3203
Cdd:PRK01156  678 diedNLKKSRKalddAKANRARLESTIEILRTRINELSDRINDINETLE 726
SPEC smart00150
Spectrin repeats;
797-863 4.06e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.01  E-value: 4.06e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767917    797 HQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFGETVATLQRRAQTVV 863
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD--LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI 65
SPEC smart00150
Spectrin repeats;
4519-4624 4.70e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 4.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917   4519 REFNDAWSGMMQYLQETEQVLdqiiEEATASKEPQKIKKYIGKLKETHRQLGAKQSVYDGTMRTGKNLLERAPkGDRPVL 4598
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL----ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 386767917   4599 DKMLIELKEQWTRVWSKSIDRQRKLE 4624
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1571-1769 4.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1571 LEVIQREISEAESGYETAEKRIKQAVfEKFNMCEENVNDLLKWVTTVEQKISSVggpREKIDELRNQINALKQikdEIES 1650
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALL-KQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRA---ELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 1651 QQRPVAtclEQIRQIVLTGGD-----VLSAPEVTTLENSGRELRSRVDRVNDRTVRL---LRRLEAGRDELTKLRSELDV 1722
Cdd:COG4942   102 QKEELA---ELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELEA 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386767917 1723 FSDWLQVARRTLE-DKERSLSDLTRLPSQADSVREFVSDVIGHQADLR 1769
Cdd:COG4942   179 LLAELEEERAALEaLKAERQKLLARLEKELAELAAELAELQQEAEELE 226
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2849-3249 4.84e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2849 AELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTN 2928
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2929 LSKPLQSLKALAKDISAEARAAGGDADHLT-SEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLE 3007
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3008 TEiEKLsppgREIKIVQVQIDDVGKIQTKLDRLVGRLEDAERAADVLVDAGFAADTTQTREQISTLRKT--LGRLDNRVR 3085
Cdd:COG4717   241 LE-ERL----KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAeeLQALPALEE 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3086 DHEDNLHSTLKALR----EFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAG 3161
Cdd:COG4717   316 LEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3162 R------------DLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQealAGLSKWLSDTEEM 3229
Cdd:COG4717   396 EyqelkeeleeleEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE---AELEQLEEDGELA 472
                         410       420
                  ....*....|....*....|
gi 386767917 3230 VANQKppssdYKVVKAQLQE 3249
Cdd:COG4717   473 ELLQE-----LEELKAELRE 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1571-1857 5.03e-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: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1571 LEVIQREISEAESGYETAEKRIkQAVFEKFNMCEENVNDLlkwvttvEQKISsvggpREKIDELRNQINALKQIKDEIES 1650
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDL-------EARLS-----HSRIPEIQAELSKLEEEVSRIEA 812
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1651 QQRPVATCLEQirqivltggdvlSAPEVTTLENSGRELRSRVDRVNDRTVRLLRRLEAGRDELTKLRSELDVfsdwLQVA 1730
Cdd:TIGR02169  813 RLREIEQKLNR------------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE----LEAA 876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1731 RRTLEDKersLSDLTRlpsqadsvrefvsDVIGHQADLRFITMAAQKF---VDESKEFLAILNDFRTSLPERLPHVEPLS 1807
Cdd:TIGR02169  877 LRDLESR---LGDLKK-------------ERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPK 940
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386767917  1808 SAESPIRQEVslvsAQYKDLLNRVNALQDRVSGLG----GRQREYQDALDKANE 1857
Cdd:TIGR02169  941 GEDEEIPEEE----LSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDE 990
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1964-2066 5.72e-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: 39.61  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1964 QDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVESNL 2043
Cdd:pfam00435    8 RDADD-LESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 386767917  2044 NDVTVKFEKLYEKANKRGEFLDD 2066
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2801-3133 5.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2801 SKAKLETRLRDLQTFRSEVWKHSGEFENT-------KGLGETFLSSCDIdKEPIKAELQDIR---DRWERLNNDLIARAH 2870
Cdd:PRK03918  253 SKRKLEEKIRELEERIEELKKEIEELEEKvkelkelKEKAEEYIKLSEF-YEEYLDELREIEkrlSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2871 EIENCSRRLDDFNDELRNLDHSLGRCEdrlaahdalggaaKDPKLLERVKAIREELTNLSKPLQSLKAlaKDISAEARAA 2950
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELE-------------ERHELYEEAKAKKEELERLKKRLTGLTP--EKLEKELEEL 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2951 GGDADHLTSEVDGLADRMSELQGRLDDR---CGELQSAATAVSQFN---------EQMKSLGIDLNDLETEIEKLSPPGR 3018
Cdd:PRK03918  397 EKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGrelteehrkELLEEYTAELKRIEKELKEIEEKER 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3019 EIKIVQVQIDDVGKIQTKLDRL---------------VGRLEDAERAA----------------------DVLVDAGFAA 3061
Cdd:PRK03918  477 KLRKELRELEKVLKKESELIKLkelaeqlkeleeklkKYNLEELEKKAeeyeklkekliklkgeikslkkELEKLEELKK 556
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767917 3062 DTTQTREQISTLRKTLGRLDNRVRD----HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIR 3133
Cdd:PRK03918  557 KLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1994-2187 9.38e-03

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: 42.74  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  1994 RLQEQIREHK--VLLADLQSHQASIDSVQVSAKhllasaSNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRL 2071
Cdd:TIGR02168  217 ELKAELRELElaLLVLRLEELREELEELQEELK------EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917  2072 SRYLDEISTVEQRMASLQEALDSRETSLLSTE-----------ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDvt 2140
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEaqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELE-- 368
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 386767917  2141 dtgVLRDRIKALESQWRNINisiDERAKLSKQKAEQQLAYEGLKDQV 2187
Cdd:TIGR02168  369 ---ELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARL 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2630-3316 9.70e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2630 RADVNSRVAALEKQ------YLALQKKLDTKKAEtEASLRDgrhfaENCSKTLGWLGGELSNLTDRLLVsahkptLQHQI 2703
Cdd:COG1196   195 LGELERQLEPLERQaekaerYRELKEELKELEAE-LLLLKL-----RELEAELEELEAELEELEAELEE------LEAEL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2704 DTHEpiyREVMAREHEVIMLINKGKDLtdRQQDRGVKRDLDRIQQQWEKLRREAVDRHTRLQtcmehckkysQTSETFLA 2783
Cdd:COG1196   263 AELE---AELEELRLELEELELELEEA--QAEEYELLAELARLEQDIARLEERRRELEERLE----------ELEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2784 WLRTAEDKLADLTPGVLSKAKLETRLRDLQTFRSEVWKHSGEFEntkglgetflsscdidkepikAELQDIRDRWERLNN 2863
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---------------------AELAEAEEELEELAE 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2864 DLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAhdalggaakdpkLLERVKAIREELTNLSKPLQSLKALAKDI 2943
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE------------LEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 2944 SAEARAAGGDADHLTSEVDGLADRMSELQGRLDdrcgelqsAATAVSQFNEQMKSLGIDLNDLETEIEKLSPPGREIKIV 3023
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELA--------EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3024 QVQIDDVGKIQTKL---------DRLVGRLEDAERAADVLVD-----AGFAADTTQTREQISTLRKTLGRLDNRVRDHED 3089
Cdd:COG1196   527 AVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAakagrATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3090 NLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFRNF-----RERKVEPLAINVDKVNVAGRDL 3164
Cdd:COG1196   607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGgsltgGSRRELLAALLEAEAELEELAE 686
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767917 3165 VRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDTEEMVANQKPPSSDYKVVK 3244
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767917 3245 AQLQEqkfLKKMLldrqNSMGSLaNLgkevanhcepgerASIEkQLNDLMKRFDALTdgaEQRElDLEEAME 3316
Cdd:COG1196   767 RELER---LEREI----EALGPV-NL-------------LAIE-EYEELEERYDFLS---EQRE-DLEEARE 812
 
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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