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Conserved domains on  [gi|221330227|ref|NP_001137657|]
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short stop, isoform I [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
36-140 4.47e-74

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409037  Cd Length: 105  Bit Score: 242.69  E-value: 4.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   36 DAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21188     1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHFQ 140
Cdd:cd21188    81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
153-257 1.93e-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: 1.93e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5020-5092 3.25e-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: 3.25e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330227   5020 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5092
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4113-4332 4.99e-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: 120.63  E-value: 4.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4113 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4192
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4193 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4272
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4273 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4332
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-859 1.75e-25

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 102.34  E-value: 1.75e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227   794 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 859
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4334-4553 6.14e-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: 105.99  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4334 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4413
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4414 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4493
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4494 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4553
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3899-4111 2.49e-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: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3899 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 3978
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3979 DLDNAWDNITALYAKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMV 4058
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 4059 EVEALNRQAVELTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHAL 4111
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3571-3781 4.07e-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: 103.68  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3571 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3650
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3651 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3730
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 3731 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3781
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4558-4766 4.70e-23

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.60  E-value: 4.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4558 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4635
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4636 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4715
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 4716 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4766
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
620-796 1.44e-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: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  620 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 699
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  700 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 779
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 221330227  780 ETVATLQRRAQTVVPLN 796
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3028-3245 1.90e-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: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3028 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3107
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3108 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3187
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 3188 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3245
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2596-2805 2.30e-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: 89.81  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2596 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2673
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2674 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2753
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2754 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2703-2915 2.00e-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: 87.12  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2703 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2782
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2783 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2862
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2863 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2915
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3248-3463 5.50e-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: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3248 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3327
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3328 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3407
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 3408 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3463
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1889-2098 1.27e-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: 82.11  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1889 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 1968
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1969 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2046
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 2047 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2098
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3781-4002 2.62e-16

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3781 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3860
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3861 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 3940
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 3941 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4002
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3465-3672 6.95e-15

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3465 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3535
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3536 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3615
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227 3616 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3672
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2378-2592 2.66e-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: 75.17  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2378 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2457
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2458 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2534
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 2535 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2592
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1083-1320 3.44e-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: 63.23  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1083 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1162
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1163 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1242
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 1243 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1320
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Metaviral_G super family cl26626
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
5230-5367 7.80e-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.


The actual alignment was detected with superfamily member pfam09595:

Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 61.51  E-value: 7.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5230 SKPPSRHGSTLSLDSTDDhtPSRIPQRKPSTGSTASGTTPRPARLSVTTTTTPGSRLNGTStitrKTASGSASPAPTSNg 5309
Cdd:pfam09595   33 LILIGESNKEAALIITDI--IDININKQHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNN----QHPSQDRSEAPPLE- 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227  5310 gmSRSSSIPALTgfgfkpiRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPT 5367
Cdd:pfam09595  106 --PAAKTKPSEH-------EPA-NPPDASNRLSPPDASTAAIREARTFRKPSTGKRNN 153
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
401-619 1.06e-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: 55.91  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  401 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 473
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  474 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 553
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  554 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 619
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
977-1180 2.00e-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: 55.14  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  977 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1052
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1053 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1126
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 221330227 1127 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1180
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
5111-5318 2.30e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.87  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5111 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5190
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5191 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5266
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5267 TTP-------RPARLSVTTTTTPGSrlnGTSTITRKTASGSASPAPTSN-GGMSRSSSIP 5318
Cdd:PHA03307  360 ADPssprkrpRPSRAPSSPAASAGR---PTRRRARAAVAGRARRRDATGrFPAGRPRPSP 416
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4945-5014 7.75e-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: 48.63  E-value: 7.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4945 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5014
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
273-482 2.69e-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: 48.60  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  273 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 352
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  353 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 432
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227  433 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 482
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1558-2116 4.37e-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: 4.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1558 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1623
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1624 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1697
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1698 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1775
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1776 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1831
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1832 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1890
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1891 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 1941
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1942 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2012
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2013 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2088
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 221330227  2089 INISIDERAKLSKQKAEQQLAYEGLKDQ 2116
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
PLEC smart00250
Plectin repeat;
1428-1456 9.67e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 9.67e-04
                            10        20
                    ....*....|....*....|....*....
gi 221330227   1428 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1456
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
36-140 4.47e-74

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 242.69  E-value: 4.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   36 DAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21188     1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHFQ 140
Cdd:cd21188    81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
153-257 1.93e-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: 1.93e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-258 4.54e-44

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 172.82  E-value: 4.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDAIQKKTFTKWVNKHL-KKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRYK 108
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  109 KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISDIvvGKEDNVSAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAF 187
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI--NEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221330227  188 SALVHRNRPDLLDWRKARNDRPRERLET--AFHIVEKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVFPE 258
Cdd:COG5069   161 SALIHDSRPDTLDPNVLDLQKKNKALNNfqAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGL 234
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5020-5092 3.25e-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: 3.25e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330227   5020 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5092
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
5022-5090 2.54e-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: 2.54e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221330227  5022 IHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRA 5090
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4113-4332 4.99e-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: 120.63  E-value: 4.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4113 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4192
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4193 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4272
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4273 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4332
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
37-141 1.74e-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: 103.91  E-value: 1.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    37 AIQKKTFTKWVNKHLKKANRRVV--DLFEDLRDGHNLLSLLEVLSGEHLP-REKGKMRFHMLQNAQMALDFLRYK-KIKL 112
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRvtNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 221330227   113 VNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-859 1.75e-25

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 102.34  E-value: 1.75e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227   794 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 859
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4334-4553 6.14e-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: 105.99  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4334 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4413
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4414 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4493
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4494 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4553
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
153-257 6.86e-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: 102.36  E-value: 6.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   153 SAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK--ARNDRPRERLETAFHIVEKEYGVTR- 228
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 221330227   229 LLDPEDVdtNEPDEKSLITYISSLYDVFP 257
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3899-4111 2.49e-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: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3899 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 3978
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3979 DLDNAWDNITALYAKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMV 4058
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 4059 EVEALNRQAVELTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHAL 4111
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3571-3781 4.07e-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: 103.68  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3571 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3650
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3651 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3730
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 3731 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3781
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
41-138 3.24e-23

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: 97.00  E-value: 3.24e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227     41 KTFTKWVNKHLKKANRRVV-DLFEDLRDGHNLLSLLEVLSGEHLPREK---GKMRFHMLQNAQMALDFLRYKKIKLVNIR 116
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVtNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 221330227    117 AEDIVDGnPKLTLGLIWTIILH 138
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4558-4766 4.70e-23

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.60  E-value: 4.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4558 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4635
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4636 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4715
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 4716 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4766
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
620-796 1.44e-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: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  620 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 699
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  700 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 779
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 221330227  780 ETVATLQRRAQTVVPLN 796
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3028-3245 1.90e-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: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3028 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3107
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3108 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3187
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 3188 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3245
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2596-2805 2.30e-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: 89.81  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2596 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2673
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2674 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2753
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2754 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
156-252 3.63e-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: 85.45  E-value: 3.63e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    156 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKAR----NDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 221330227    232 PEDVDTNEPDEKSLITYISSL 252
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2703-2915 2.00e-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: 87.12  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2703 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2782
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2783 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2862
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2863 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2915
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3248-3463 5.50e-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: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3248 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3327
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3328 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3407
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 3408 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3463
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1889-2098 1.27e-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: 82.11  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1889 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 1968
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1969 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2046
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 2047 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2098
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3781-4002 2.62e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3781 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3860
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3861 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 3940
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 3941 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4002
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3465-3672 6.95e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3465 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3535
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3536 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3615
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227 3616 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3672
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4116-4218 1.02e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 72.75  E-value: 1.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4116 QFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIetEKGSVEASTTQEK 4195
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 221330227   4196 LRKLNNEWKQLLQKASDRQHELE 4218
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2378-2592 2.66e-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: 75.17  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2378 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2457
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2458 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2534
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 2535 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2592
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4112-4219 8.31e-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: 67.73  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4112 LHLGQFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEAST 4191
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 221330227  4192 TQEKLRKLNNEWKQLLQKASDRQHELEE 4219
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4007-4108 1.13e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 1.13e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4007 EFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTERtSPEQAASIREPL 4086
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   4087 SVVNRRWEALLRGMVERQKQLE 4108
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4558-4656 2.01e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 2.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4558 QFSDALGELLDWLKKAKSRLnENGPVHGDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4635
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   4636 EMQSIWEEVKSAVAKRGERLQ 4656
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
621-721 1.41e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 1.41e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    621 QHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHLT 700
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227    701 ALQQQWAWLLQLTLCLEVHLK 721
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1083-1320 3.44e-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: 63.23  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1083 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1162
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1163 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1242
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 1243 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1320
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3541-4225 4.62e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 4.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3541 NRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADlpamepKLVRAQLQEHRSINDDISSQKGRV 3620
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ------KELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3621 RDVTAASKKV---LRESPQS-----ENTATLREKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDM 3692
Cdd:TIGR02168  312 ANLERQLEELeaqLEELESKldelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3693 EQQISRLSMPALRPD-QITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALvaDDDGAKINEILDTDNARYAALRLE 3769
Cdd:TIGR02168  392 ELQIASLNNEIERLEaRLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3770 LRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPLSAL---PQKIREQIED------ND 3826
Cdd:TIGR02168  470 LEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVLSELisvDEGYEAAIEAalggrlQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3827 ALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA---------------VRDIKAKLEKLNNLW-------N 3876
Cdd:TIGR02168  550 VVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvakdLVKFDPKLRKALSYLlggvlvvD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3877 DVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEETLscqeppAAQPQDIKKQQVALQEI 3940
Cdd:TIGR02168  630 DLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEKI------EELEEKIAELEKALAEL 703
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3941 RHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLQNLLKFLT 4020
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4021 KAEDKFAHLGAvgsDIDAVKRQIEQLKSfkdevdphmvEVEALNRQAVELTERtspeqAASIREPLSVVNRRWEALLRGM 4100
Cdd:TIGR02168  779 EAEAEIEELEA---QIEQLKEELKALRE----------ALDELRAELTLLNEE-----AANLRERLESLERRIAATERRL 840
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4101 VERQKQLEHALLHLGQFQHALNELLVWINKtdstldqlkpipgdpqlLEVELAKLKVLANDIQAHQNSV-DTLNDAGRQL 4179
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEE-----------------LESELEALLNERASLEEALALLrSELEELSEEL 903
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*.
gi 221330227  4180 IETEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALREAH 4225
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
SPEC smart00150
Spectrin repeats;
4337-4438 7.19e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 7.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4337 EFHDTLQAFVEWLTQAEKLLSnAEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIKNLL 4416
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   4417 VSVQHRWERVVSKAAERTRALD 4438
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
5230-5367 7.80e-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: 7.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5230 SKPPSRHGSTLSLDSTDDhtPSRIPQRKPSTGSTASGTTPRPARLSVTTTTTPGSRLNGTStitrKTASGSASPAPTSNg 5309
Cdd:pfam09595   33 LILIGESNKEAALIITDI--IDININKQHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNN----QHPSQDRSEAPPLE- 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227  5310 gmSRSSSIPALTgfgfkpiRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPT 5367
Cdd:pfam09595  106 --PAAKTKPSEH-------EPA-NPPDASNRLSPPDASTAAIREARTFRKPSTGKRNN 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2771-3296 9.32e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2771 DIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDpkLLERVK 2850
Cdd:PRK02224  191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED--LRETIA 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2851 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 2930
Cdd:PRK02224  269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2931 IDLNDLETEIEKLSPPGREI-KIVQVQIDDVGKIQTKLDRLVGRLEDAERAADvlvdagfaaDTTQTREQISTLRKTLGR 3009
Cdd:PRK02224  349 EDADDLEERAEELREEAAELeSELEEAREAVEDRREEIEELEEEIEELRERFG---------DAPVDLGNAEDFLEELRE 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3010 LDNRVRDHEDNLHSTLKALREFYDHQSQTLDD------IQDVSDEfkrmkPVGSELDQIRRQQEDFrnfrERKVEPLAIN 3083
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGS-----PHVETIEEDRERVEEL----EAELEDLEEE 490
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3084 VDKVNvagrDLVRSAGSGVSTtaiEKDLEKLNDRWNDLKERMNERDRRLDvallqsgKFQEALAGLSKWLSDTE-EMVAN 3162
Cdd:PRK02224  491 VEEVE----ERLERAEDLVEA---EDRIERLEERREDLEELIAERRETIE-------EKRERAEELRERAAELEaEAEEK 556
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3163 QKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVAnhcepgERASIEKQLNDLMKRFDALTDGAEQRELDLE 3242
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA------AIADAEDEIERLREKREALAELNDERRERLA 630
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 3243 EAMEVAKRFHDKISP--LELWLDNTERSVKAMELIptdEEKIQQRIREHDRLHDEI 3296
Cdd:PRK02224  631 EKRERKRELEAEFDEarIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEI 683
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5120-5365 3.34e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.04  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5120 STPNAAATASSSPHAHNGGSSN---LPPYMSGQGPIIKVRERSVRSIP-----MSRPSRSSLSASTPDSLSDNEGSHGGP 5191
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPpaaASPRPPRRSSPISASASSPAPAPgrsaaDDAGASSSDSSSSESSGCGWGPENECP 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5192 SGRYTPrKVTYTSTRTGLTPG--GSRAGSKPNSRPLSRQGSKPPSRHGSTLSLDSTDDHTPSRIPQRKPSTGST------ 5263
Cdd:PHA03307  257 LPRPAP-ITLPTRIWEASGWNgpSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTsssses 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5264 ----ASGTTPRPARLSvtTTTTPGSRLNGTSTITRKTASGSASPAPTSNGGMSRSSSIPALTGFGfkpiRRNISGSSTPS 5339
Cdd:PHA03307  336 srgaAVSPGPSPSRSP--SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRA----RRRDATGRFPA 409
                         250       260
                  ....*....|....*....|....*.
gi 221330227 5340 GMQTPRKSSAEPTFSSTMRRTSRGTT 5365
Cdd:PHA03307  410 GRPRPSPLDAGAASGAFYARYPLLTP 435
SPEC smart00150
Spectrin repeats;
3676-3778 5.37e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 5.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3676 EHFADSHQGLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3755
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 221330227   3756 LDTDNARYAALRLELRERQQALE 3778
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3141-3242 6.78e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 6.78e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3141 KFQEALAGLSKWLSDTEEMVAnQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPgERASIEKQL 3220
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   3221 NDLMKRFDALTDGAEQRELDLE 3242
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
401-619 1.06e-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: 55.91  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  401 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 473
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  474 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 553
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  554 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 619
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
977-1180 2.00e-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: 55.14  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  977 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1052
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1053 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1126
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 221330227 1127 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1180
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5111-5318 2.30e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.87  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5111 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5190
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5191 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5266
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5267 TTP-------RPARLSVTTTTTPGSrlnGTSTITRKTASGSASPAPTSN-GGMSRSSSIP 5318
Cdd:PHA03307  360 ADPssprkrpRPSRAPSSPAASAGR---PTRRRARAAVAGRARRRDATGrFPAGRPRPSP 416
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
620-713 3.20e-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: 51.55  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   620 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 699
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 221330227   700 TALQQQWAWLLQLT 713
Cdd:pfam00435   83 EELNERWEQLLELA 96
SPEC smart00150
Spectrin repeats;
3250-3350 6.62e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 6.62e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3250 RFHDKISPLELWLDNTERSVKAMElIPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGEKV 3329
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   3330 RGVTERYTGLVDASDNIGALL 3350
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
289-615 8.42e-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: 8.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   289 REKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYFETVGEVDVEAELrpdaiekawyrmn 368
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------- 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   369 taLQDREvilQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEGRRIERLhpvdaKSIVEALETEIRHleEPIQD 448
Cdd:TIGR02169  728 --LEQEE---EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-----EEALNDLEARLSH--SRIPE 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   449 MNQ------DCHVLNEGRyphVSELHKKVNKLHQRWAQLRtnfhtnlvQKLSGLKYPVHETTVTRQTRmvvESRQIDTNP 522
Cdd:TIGR02169  796 IQAelskleEEVSRIEAR---LREIEQKLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSI---EKEIENLNG 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   523 HFRDLQEHIEWCQNKLKQLlaADYGSDLPSVKEELDRQQHEHKI-IDQFHTKIlNDERQQTKFSGDELALYQQRLNQLQK 601
Cdd:TIGR02169  862 KKEELEEELEELEAALRDL--ESRLGDLKKERDELEAQLRELERkIEELEAQI-EKKRKRLSELKAKLEALEEELSEIED 938
                          330
                   ....*....|....
gi 221330227   602 VYAELLSTSTKRLS 615
Cdd:TIGR02169  939 PKGEDEEIPEEELS 952
SPEC smart00150
Spectrin repeats;
2703-2803 1.11e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   2703 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2782
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   2783 DIRDRWERLNNDLIARAHEIE 2803
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4333-4437 2.92e-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: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4333 KEATEFHDTLQAFVEWLTQAEKLLSNaEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKYfSQKQDVILI 4412
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 221330227  4413 KNLLVSVQHRWERVVSKAAERTRAL 4437
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3967-4297 3.24e-06

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: 53.92  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3967 EPDK-PEVKKHIEDLDNAWDNITALYAKREE---NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAH-LGAVGSDIDAVKR 4041
Cdd:TIGR02169  672 EPAElQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4042 QIEQLKSFKDEVDPHMVEVE----ALNRQAVELTERTSPEQAASIREPLSVVN---RRWEALLRGmVERQKQLEHALLHL 4114
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEedlhKLEEALNDLEARLSHSRIPEIQAELSKLEeevSRIEARLRE-IEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4115 GQ--FQHALNELLVWINKTDSTLDQLKPIPGDPQLLEVELAKLKVLANDIQA-HQNSVDTLNDAGRQLIETEKGSVEAST 4191
Cdd:TIGR02169  831 LEkeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrLGDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4192 TQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEVQDilgwLGDVDAV-------IGASKPVGGLpetATEQLER 4264
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAElqrveeeIRALEPVNML---AIQEYEE 983
                          330       340       350
                   ....*....|....*....|....*....|...
gi 221330227  4265 FMEVYNELDENRPKVETIQAQGQEYIKRQNQMK 4297
Cdd:TIGR02169  984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4558-4656 3.47e-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: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4558 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSGN--NPEVGRQLD 4635
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHyaSEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 221330227  4636 EMQSIWEEVKSAVAKRGERLQ 4656
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
3786-3890 4.05e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 4.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3786 QFSDKLEGMLRALANTVDQVNQlDPLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIakagNKADPAVRDIK 3865
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI----EEGHPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   3866 AKLEKLNNLWNDVQNATKKRGSSLD 3890
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4032-4108 4.61e-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: 48.47  E-value: 4.61e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227  4032 VGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTERtSPEQAASIREPLSVVNRRWEALLRGMVERQKQLE 4108
Cdd:pfam00435   29 YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLE 104
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4945-5014 7.75e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.63  E-value: 7.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4945 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5014
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SPEC smart00150
Spectrin repeats;
1891-1995 1.66e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 1.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   1891 QGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVE 1970
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD--AEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   1971 SNLNDVTVKFEKLYEKANKRGEFLD 1995
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2837-3250 2.19e-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: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2837 GGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAA 2916
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2917 TAVSQFNEQMKSLGIDLNDLETEIEKLsppgreIKIVQVQIDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaadTTQT 2996
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKEL------EARIEELEEDLHKLEEALNDLEARLSHSR--------------IPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2997 REQISTLRKTLGRLDNRVRDHEDNLHStLKALREFYDHQSQTLDDIQDVSDEFKRMkpvgseldqIRRQQEDFRNFRERK 3076
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKS---------IEKEIENLNGKKEEL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3077 VEPLAinvdKVNVAGRDLVRSAGSgvsttaIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDT 3156
Cdd:TIGR02169  867 EEELE----ELEAALRDLESRLGD------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3157 EEMVANQKPPSS---DYKVVKAQLQEqkflkkmLLDRQNSMGSLANLGKEvanhcepgERASIEKQLNDLMKRFDALTdg 3233
Cdd:TIGR02169  937 EDPKGEDEEIPEeelSLEDVQAELQR-------VEEEIRALEPVNMLAIQ--------EYEEVLKRLDELKEKRAKLE-- 999
                          410
                   ....*....|....*...
gi 221330227  3234 AEQREL-DLEEAMEVAKR 3250
Cdd:TIGR02169 1000 EERKAIlERIEEYEKKKR 1017
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
273-482 2.69e-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: 48.60  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  273 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 352
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  353 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 432
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227  433 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 482
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3571-3670 2.84e-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: 46.16  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3571 DIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPQSenTATLREKLDDL 3650
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 221330227  3651 KEIVDTVAQLCSERLGILEQ 3670
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2382-2482 3.16e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 3.16e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   2382 FLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAVEIKL 2461
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   2462 KDILGKWDDLVGKLDDRANSL 2482
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1558-2116 4.37e-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: 4.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1558 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1623
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1624 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1697
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1698 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1775
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1776 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1831
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1832 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1890
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1891 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 1941
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1942 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2012
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2013 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2088
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 221330227  2089 INISIDERAKLSKQKAEQQLAYEGLKDQ 2116
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
EF-hand_7 pfam13499
EF-hand domain pair;
4943-5007 5.81e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 5.81e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227  4943 KSRLTDLFRKMDKDNNGMIPRDVFIDGI--LNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5007
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
4945-5007 7.77e-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: 7.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330227 4945 RLTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5007
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3141-3243 8.04e-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: 8.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3141 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcEPGERASIEKQL 3220
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 221330227  3221 NDLMKRFDALTDGAEQRELDLEE 3243
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2669-3023 1.50e-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: 48.53  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2669 VKRDLDRIQQQWEKLR---REAVDRHTRLQTCMEHCKKYSqtsetflawlrtaedkladltpgvlskaKLETRLRDLqtf 2745
Cdd:TIGR02169  175 ALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQ----------------------------ALLKEKREY--- 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2746 rsEVWKHSGEFENT---KGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCS--------RRLDDFND 2814
Cdd:TIGR02169  224 --EGYELLKEKEALerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEA 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2815 ELRNLDHSLGRCEDRLaaHDAlggAAKDPKLLERVKAIREELTNLSKPLQSLKAlakdisaearaaggdadhltsEVDGL 2894
Cdd:TIGR02169  302 EIASLERSIAEKEREL--EDA---EERLAKLEAEIDKLLAEIEELEREIEEERK---------------------RRDKL 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2895 ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEKLSPPGREIKIVQVQID-DVGKIQTKLDRLVGR 2973
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeELADLNAAIAGIEAK 435
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 221330227  2974 LEDAERAADVLVDAGFAADT--TQTREQISTLRKTLGRLDNRVRDHEDNLHS 3023
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
SPEC smart00150
Spectrin repeats;
524-618 1.79e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    524 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 600
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVeaLNELGEQLIEEGHPDAEEiEERLEELN 83
                            90
                    ....*....|....*...
gi 221330227    601 KVYAELLSTSTKRLSDLD 618
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3467-3558 2.15e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 2.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3467 QQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIESIV 3537
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAsedlGKDLESVEALlkkheAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   3538 TRDNRRFDSIVEQIQRKAERL 3558
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2773-3030 2.35e-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: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2773 DKEPIKAELQDIRDRWERLNndliaRAHE-IENCSRRLDDFnDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKA 2851
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLE-----RAHEaLEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2852 IREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGL-ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 2930
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2931 IDLNDLETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLVDAgFAADTTQTREQISTLRKTLGRL 3010
Cdd:COG4913   373 LPLPASAEEFAAL--------------------RAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASL 431
                         250       260
                  ....*....|....*....|
gi 221330227 3011 DNRVRDHEDNLHSTLKALRE 3030
Cdd:COG4913   432 ERRKSNIPARLLALRDALAE 451
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
815-852 2.55e-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: 2.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 221330227  815 KQQGQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIP 852
Cdd:cd11768    11 IEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIP 48
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1642-1887 2.78e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1642 ELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKFVDESKEflailnd 1721
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1722 frtslperlphveplssAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDkANEWLRSvhpRVSRIIS 1801
Cdd:cd00176    73 -----------------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEE---KEAALAS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1802 EPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSlggqLSPMEINQLELPIADLKNNYQQLLDNLGEHCK 1881
Cdd:cd00176   132 EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQK 207

                  ....*.
gi 221330227 1882 TLDKTL 1887
Cdd:cd00176   208 KLEEAL 213
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-497 3.63e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  306 EMKRLLSDLQRFRSDEVSARKREK------------SKLIQIYKELERYFETVGEVDVEaELRPDA--IEKAWYRMNTaL 371
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLE-ELEKKAeeYEKLKEKLIK-L 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  372 QDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEG--------RRIERLHP--------VDAKSIVEAL 435
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleERLKELEPfyneylelKDAEKELERE 617
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227  436 ETEIRHLEEPIQDMNQDCHVLNEgrypHVSELHKKVNKLHQRWAQLR----TNFHTNLVQKLSGLK 497
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEK----RLEELRKELEELEKKYSEEEyeelREEYLELSRELAGLR 679
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1929-2111 3.91e-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: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1929 IREHKVLLADLQSHQASIDSVQVSAKHLLASASNARI--AKKVESNLNDVtvkfekLYEKANKRGEFLDDVYNRLSRYLD 2006
Cdd:COG5391   303 FSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGvfAKRLEQNQNSI------LNEGVVQAETLRSSLKELLTQLQD 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2007 EISTVEQRMASLQEALDSRETSLLSTEELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQW 2086
Cdd:COG5391   377 EIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDK 456
                         170       180       190
                  ....*....|....*....|....*....|
gi 221330227 2087 RNI----NISIDERAKLSKQ-KAEQQLAYE 2111
Cdd:COG5391   457 EKLeeqlAIAEKDAQEINEElKNELKFFFS 486
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
808-856 4.55e-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: 4.55e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 221330227    808 VQAICAYKQQ--GQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACL 856
Cdd:smart00326    5 VRALYDYTAQdpDELSFKKGDIITVLEKSDDGWWKGRLGRGKEGLFPSNYV 55
PLEC smart00250
Plectin repeat;
1428-1456 9.67e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 9.67e-04
                            10        20
                    ....*....|....*....|....*....
gi 221330227   1428 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1456
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1496-2008 1.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1496 RELSLLEVIQREISEAESGYETAEKRIKqAVFEKFNMCEENVNDLLKWVTTVEQKIssvGGPREKIDELRNQINALKQIK 1575
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1576 DEIESQqRPVATCLEQIRQIVLTGGDVLSAPEV--TTLENSGRELRSRVDRVNDRTVRLlRRLEAGRDELTKLRSELDVF 1653
Cdd:PRK03918  283 KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKrlSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1654 SDWLQVARRTLEDKERSLSDLTRLPSQaDSVREfvsdvighqadLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHV 1733
Cdd:PRK03918  361 HELYEEAKAKKEELERLKKRLTGLTPE-KLEKE-----------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1734 EPLSSAES-------PIRQE-----VSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDKAN---------EWLRSV 1792
Cdd:PRK03918  429 EELKKAKGkcpvcgrELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKEL 508
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1793 HPRVSRIISEP-----------------IAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSLGgQLSPMEI 1855
Cdd:PRK03918  509 EEKLKKYNLEElekkaeeyeklkeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1856 NQLELPIADLKNNY-------------QQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIK 1922
Cdd:PRK03918  588 EELEERLKELEPFYneylelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELR 665
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1923 ERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANK-RGEFLDDVYNRL 2001
Cdd:PRK03918  666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKyKALLKERALSKV 745

                  ....*..
gi 221330227 2002 SRYLDEI 2008
Cdd:PRK03918  746 GEIASEI 752
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3604-3872 1.38e-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: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3604 QEHRSINDDISSQKGRVRDVTAASKKVLRESPQSENTATLREKLDDLKEIVDTVAQLcSERLGILEQALPLSEHFADSHQ 3683
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3684 GLTAWLDDMEQQISRLSmpalrpDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEAlgALVADDDGAKINEILDtdnARY 3763
Cdd:COG4913   696 ELEAELEELEEELDELK------GEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGD---AVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3764 AALRLELRERQQALESALQESSQfsdKLEGMLRALANT-VDQVNQLDP-LSALP--QKIREQIEDndalmDDL-DKRQDA 3838
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEE---ELERAMRAFNREwPAETADLDAdLESLPeyLALLDRLEE-----DGLpEYEERF 836
                         250       260       270
                  ....*....|....*....|....*....|....
gi 221330227 3839 FSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLN 3872
Cdd:COG4913   837 KELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
916-1099 1.67e-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: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   916 EQRTAIRRALNDDA--DKLLSEGDPNDPQLRRLRRE----MDEVNRLFDEFEK-RARAEEESKQASRIFtEECLAIKSKL 988
Cdd:TIGR02169  316 ELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDlRAELEEVDKEFAETR-DELKDYREKL 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   989 EDMARELDQIIlAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALKtpvLKKSLDNLMELWKELNTQsgl 1068
Cdd:TIGR02169  395 EKLKREINELK-RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSKY--- 467
                          170       180       190
                   ....*....|....*....|....*....|.
gi 221330227  1069 hKDRLKLLEASLAGLEDNehvISELENELAR 1099
Cdd:TIGR02169  468 -EQELYDLKEEYDRVEKE---LSKLQRELAE 494
SPEC smart00150
Spectrin repeats;
1083-1183 1.71e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 1.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   1083 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1162
Cdd:smart00150    7 ADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   1163 RLNTRWSAVCNQLGERMRSCE 1183
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3250-3344 2.11e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3250 RFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKV 3329
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERL 82
                           90
                   ....*....|....*
gi 221330227  3330 RGVTERYTGLVDASD 3344
Cdd:pfam00435   83 EELNERWEQLLELAA 97
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1501-1699 4.50e-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: 43.21  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1501 LEVIQREISEAESGYETAEKRIKQAVfEKFNMCEENVNDLLKWVTTVEQKISSVggpREKIDELRNQINALKQikdEIES 1580
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALL-KQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRA---ELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1581 QQRPVAtclEQIRQIVLTGGD-----VLSAPEVTTLENSGRELRSRVDRVNDRTVRL---LRRLEAGRDELTKLRSELDV 1652
Cdd:COG4942   102 QKEELA---ELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELEA 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 221330227 1653 FSDWLQVARRTLE-DKERSLSDLTRLPSQADSVREFVSDVIGHQADLR 1699
Cdd:COG4942   179 LLAELEEERAALEaLKAERQKLLARLEKELAELAAELAELQQEAEELE 226
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2731-3063 6.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2731 SKAKLETRLRDLQTFRSEVWKHSGEFENT-------KGLGETFLSSCDIdKEPIKAELQDIR---DRWERLNNDLIARAH 2800
Cdd:PRK03918  253 SKRKLEEKIRELEERIEELKKEIEELEEKvkelkelKEKAEEYIKLSEF-YEEYLDELREIEkrlSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2801 EIENCSRRLDDFNDELRNLDHSLGRCEdrlaahdalggaaKDPKLLERVKAIREELTNLSKPLQSLKAlaKDISAEARAA 2880
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELE-------------ERHELYEEAKAKKEELERLKKRLTGLTP--EKLEKELEEL 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2881 GGDADHLTSEVDGLADRMSELQGRLDDR---CGELQSAATAVSQFN---------EQMKSLGIDLNDLETEIEKLSPPGR 2948
Cdd:PRK03918  397 EKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGrelteehrkELLEEYTAELKRIEKELKEIEEKER 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2949 EIKIVQVQIDDVGKIQTKLDRL---------------VGRLEDAERAA----------------------DVLVDAGFAA 2991
Cdd:PRK03918  477 KLRKELRELEKVLKKESELIKLkelaeqlkeleeklkKYNLEELEKKAeeyeklkekliklkgeikslkkELEKLEELKK 556
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 2992 DTTQTREQISTLRKTLGRLDNRVRD----HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIR 3063
Cdd:PRK03918  557 KLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1894-1996 7.10e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.22  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1894 QDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVESNL 1973
Cdd:pfam00435    8 RDADD-LESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 221330227  1974 NDVTVKFEKLYEKANKRGEFLDD 1996
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1924-2117 9.71e-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: 9.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1924 RLQEQIREHK--VLLADLQSHQASIDSVQVSAKhllasaSNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRL 2001
Cdd:TIGR02168  217 ELKAELRELElaLLVLRLEELREELEELQEELK------EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2002 SRYLDEISTVEQRMASLQEALDSRETSLLSTE-----------ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDvt 2070
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEaqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELE-- 368
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 221330227  2071 dtgVLRDRIKALESQWRNINisiDERAKLSKQKAEQQLAYEGLKDQV 2117
Cdd:TIGR02168  369 ---ELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARL 409
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3756-4182 9.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3756 LDTDNARYAALRLEL---RERQQALESALQESSQFSDKLEGMLRALANTVDQV---NQLDPLSALPQKIREQIEDNDALM 3829
Cdd:COG4717    83 AEEKEEEYAELQEELeelEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELEERLEELRELE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3830 DDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWKQLNSVM-- 3907
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAle 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3908 KTLKDLEETL-------------SCQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVK 3974
Cdd:COG4717   243 ERLKEARLLLliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3975 KHIEDL----DNAWDNITALYaKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLGAvgSDIDAVKRQIEQLKSFK 4050
Cdd:COG4717   323 ELLAALglppDLSPEELLELL-DRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQ 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4051 DEVDphmvEVEALNRQaveLTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALNELlvwinK 4130
Cdd:COG4717   399 ELKE----ELEELEEQ---LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL-----E 466
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 4131 TDSTLDQLKpipgdpQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIET 4182
Cdd:COG4717   467 EDGELAELL------QELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
36-140 4.47e-74

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 242.69  E-value: 4.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   36 DAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21188     1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHFQ 140
Cdd:cd21188    81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
153-257 1.93e-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: 1.93e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
30-144 5.39e-57

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 194.82  E-value: 5.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   30 RIADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKK 109
Cdd:cd21236     9 RYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQ 88
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISDI 144
Cdd:cd21236    89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
33-146 2.61e-55

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 189.47  E-value: 2.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   33 DERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKL 112
Cdd:cd21235     1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 221330227  113 VNIRAEDIVDGNPKLTLGLIWTIILHFQISDIVV 146
Cdd:cd21235    81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 114
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
33-149 1.02e-50

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 176.38  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   33 DERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKL 112
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  113 VNIRAEDIVDGNPKLTLGLIWTIILHFQISDIVVGKE 149
Cdd:cd21237    81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
31-137 5.06e-49

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 171.40  E-value: 5.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   31 IADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLRYKK 109
Cdd:cd21246     9 LADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQR 88
                          90       100
                  ....*....|....*....|....*...
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21246    89 VHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
38-141 2.24e-46

first 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 links 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 163.32  E-value: 2.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVV-DLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNIR 116
Cdd:cd21186     2 VQKKTFTKWINSQLSKANKPPIkDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
                          90       100
                  ....*....|....*....|....*
gi 221330227  117 AEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21186    82 SNDIVDGNPKLTLGLVWSIILHWQV 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
34-141 2.69e-46

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 163.70  E-value: 2.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKHLKKANR--RVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKM--RFHMLQNAQMALDFLRYKK 109
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
30-137 1.78e-44

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 158.23  E-value: 1.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   30 RIADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLRyK 108
Cdd:cd21193     8 ALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFLK-T 86
                          90       100
                  ....*....|....*....|....*....
gi 221330227  109 KIKLVNIRAEDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21193    87 KVRLENIGAEDIVDGNPRLILGLIWTIIL 115
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-258 4.54e-44

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 172.82  E-value: 4.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDAIQKKTFTKWVNKHL-KKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRYK 108
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  109 KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISDIvvGKEDNVSAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAF 187
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI--NEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221330227  188 SALVHRNRPDLLDWRKARNDRPRERLET--AFHIVEKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVFPE 258
Cdd:COG5069   161 SALIHDSRPDTLDPNVLDLQKKNKALNNfqAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGL 234
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
153-256 9.47e-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: 9.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21194    82 EDVDVARPDEKSIMTYVASYYHYF 105
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
8-137 5.48e-41

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 149.05  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    8 SEWAKDKPLSILQLDPADRAvlrIADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-E 86
Cdd:cd21317     4 DDWDNDNSSARLFERSRIKA---LADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227   87 KGKMRFHMLQNAQMALDFLRYKKIKLVNIRAEDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21317    81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
153-256 8.95e-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: 8.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21248     2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21248    82 EDVNVEQPDEKSIITYVVTYYHYF 105
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
31-137 2.49e-40

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 147.48  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   31 IADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLRYKK 109
Cdd:cd21318    31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
                          90       100
                  ....*....|....*....|....*...
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21318   111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
5020-5092 3.25e-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: 3.25e-40
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330227   5020 DKIHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRAKG 5092
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
39-137 3.64e-40

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 145.61  E-value: 3.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLRYKKIKLVNIRA 117
Cdd:cd21214     6 QRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVSIGA 85
                          90       100
                  ....*....|....*....|
gi 221330227  118 EDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21214    86 EEIVDGNLKMTLGMIWTIIL 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
34-141 4.70e-40

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 145.79  E-value: 4.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKHLKKANRRVV--DLFEDLRDGHNLLSLLEVLSGEHLPREKGKM--RFHMLQNAQMALDFLRYKK 109
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVinDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
153-256 4.91e-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: 4.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21319    85 EDVFTENPDEKSIITYVVAFYHYF 108
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
141-256 7.52e-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: 145.20  E-value: 7.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  141 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 220
Cdd:cd21216     1 IQDISV---EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  221 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21216    78 EKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
153-257 2.56e-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: 143.23  E-value: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21243     5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21243    85 EDVDVDKPDEKSIMTYVAQFLKKYP 109
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
5022-5090 2.54e-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: 2.54e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221330227  5022 IHDEVKRLVMLCTCRQKFRVFQVGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLQKNDPCRA 5090
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
34-141 2.63e-38

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 140.74  E-value: 2.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKHLKK--ANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIK 111
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 221330227  112 LVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
153-257 2.68e-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: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 232
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21239    80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
37-139 2.49e-37

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 137.53  E-value: 2.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   37 AIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21215     3 DVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTN 82
                          90       100
                  ....*....|....*....|....*
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21215    83 IGAEDIVDGNLKLILGLLWTLILRF 107
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
151-257 7.46e-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: 7.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  151 NVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLL 230
Cdd:cd21240     2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                          90       100
                  ....*....|....*....|....*..
gi 221330227  231 DPEDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21240    81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
153-256 1.45e-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: 1.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21249     4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21249    84 EDVAVPHPDERSIMTYVSLYYHYF 107
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
153-256 3.89e-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: 134.80  E-value: 3.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21321    85 EDVNVDQPDEKSIITYVATYYHYF 108
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
152-257 6.21e-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: 6.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  152 VSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21238     1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                          90       100
                  ....*....|....*....|....*.
gi 221330227  232 PEDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
153-257 8.46e-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: 133.32  E-value: 8.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21192     3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEV 82
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21192    83 EDVLVDKPDERSIMTYVSQFLRMFP 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
33-141 1.17e-35

first 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. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 133.12  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   33 DERDAIQKKTFTKWVNKHLKKANRRVV-DLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIK 111
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIeDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 221330227  112 LVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
158-257 1.08e-34

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: 129.86  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  158 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDT 237
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
                          90       100
                  ....*....|....*....|
gi 221330227  238 NEPDEKSLITYISSLYDVFP 257
Cdd:cd21187    85 EQPDKKSILMYVTSLFQVLP 104
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
140-256 7.26e-34

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: 128.63  E-value: 7.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  140 QISDIVVGKEDNV---SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETA 216
Cdd:cd21322     1 QIQVIKIETEDNRetrSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 221330227  217 FHIVEKEYGVTRLLDPEDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21322    81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYF 120
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
158-262 1.07e-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: 127.35  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  158 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK-ARNDRPRERLETAFHIVEKEYGVTRLLDPEDVD 236
Cdd:cd21233     5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
                          90       100
                  ....*....|....*....|....*.
gi 221330227  237 TNEPDEKSLITYISSLYDVFPEPPSI 262
Cdd:cd21233    85 TAHPDKKSILMYVTSLFQVLPQQVSI 110
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
31-137 3.52e-33

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 127.85  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   31 IADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLRYKK 109
Cdd:cd21316    46 LADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQR 125
                          90       100
                  ....*....|....*....|....*...
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIIL 137
Cdd:cd21316   126 VHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
38-141 4.99e-33

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 125.48  E-value: 4.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21227     4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
                          90       100
                  ....*....|....*....|....*.
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21227    84 GNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
141-256 1.63e-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: 124.18  E-value: 1.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  141 ISDIvvgKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 220
Cdd:cd21291     1 IADI---NEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  221 EKEYGVTRLLDPEDV-DTNEPDEKSLITYISSLYDVF 256
Cdd:cd21291    78 SKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
38-142 6.20e-32

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 122.95  E-value: 6.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRY-KKIKLVN 114
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALKFLEEdEGIKIVN 94
                          90       100
                  ....*....|....*....|....*...
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21311    95 IDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
158-257 6.59e-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: 121.99  E-value: 6.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  158 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDT 237
Cdd:cd21234     5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
                          90       100
                  ....*....|....*....|
gi 221330227  238 NEPDEKSLITYISSLYDVFP 257
Cdd:cd21234    85 QLPDKKSIIMYLTSLFEVLP 104
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
153-256 9.99e-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: 121.74  E-value: 9.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21320    82 EDISVDHPDEKSIITYVVTYYHYF 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
37-141 8.15e-31

first 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 first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 118.96  E-value: 8.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   37 AIQKKTFTKWVNKHLKKANR-RVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*.
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
38-139 1.03e-30

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 118.74  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR---EKGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21183     4 IQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLVN 83
                          90       100
                  ....*....|....*....|....*
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21183    84 IGSGDIVNGNIKLILGLIWTLILHY 108
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
152-250 1.59e-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: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  152 VSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21244     4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                          90
                  ....*....|....*....
gi 221330227  232 PEDVDTNEPDEKSLITYIS 250
Cdd:cd21244    84 PEDVDVVNPDEKSIMTYVA 102
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
154-257 3.22e-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: 3.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  154 AREALLRWARRSTARYpGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 233
Cdd:cd21245     4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
                          90       100
                  ....*....|....*....|....
gi 221330227  234 DVDTNEPDEKSLITYISSLYDVFP 257
Cdd:cd21245    83 DVMVDSPDEQSIMTYVAQFLEHFP 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
34-143 3.68e-30

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 117.30  E-value: 3.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKHLKKANR--RVVDLFEDLRDGHNLLSLLEVLSGEHLPRE--KGKMRFHMLQNAQMALDFLRYKK 109
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 221330227  110 IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISD 143
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4113-4332 4.99e-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: 120.63  E-value: 4.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4113 HLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEASTT 4192
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4193 QEKLRKLNNEWKQLLQKASDRQHELEEALrEAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNEL 4272
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4273 DENRPKVETIQAQGQEYIKRQNQmkVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIAL 4332
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
156-256 5.02e-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: 116.62  E-value: 5.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  156 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPED- 234
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                          90       100
                  ....*....|....*....|..
gi 221330227  235 VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd22198    83 ASLAVPDKLSMVSYLSQFYEAF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4004-4221 2.85e-29

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 118.70  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4004 KAMEFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTERtSPEQAASIR 4083
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4084 EPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALnELLVWINKTDSTLDQLkPIPGDPQLLEVELAKLKVLANDIQ 4163
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 4164 AHQNSVDTLNDAGRQLIEtEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEAL 4221
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
153-256 3.97e-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: 114.37  E-value: 3.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21253     1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21253    81 EDmVALKVPDKLSILTYVSQYYNYF 105
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
38-139 5.48e-29

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 113.74  E-value: 5.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGK---MRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKrptFRQMKLENVSVALEFLERESIKLVS 83
                          90       100
                  ....*....|....*....|....*
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21228    84 IDSSAIVDGNLKLILGLIWTLILHY 108
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
139-256 1.17e-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: 113.64  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  139 FQISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFH 218
Cdd:cd21290     2 FAIQDISV---EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 221330227  219 IVEKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21290    79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
141-256 1.21e-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: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  141 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 220
Cdd:cd21287     1 IQDISV---EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  221 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21287    78 EKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
154-256 2.09e-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: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  154 AREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 233
Cdd:cd21197     1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                          90       100
                  ....*....|....*....|....
gi 221330227  234 D-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21197    81 DmVTMHVPDRLSIITYVSQYYNHF 104
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
141-256 3.25e-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: 3.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  141 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 220
Cdd:cd21289     1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  221 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21289    78 EKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
30-141 7.02e-28

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 111.39  E-value: 7.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   30 RIADERDAIQKKTFTKWVNKHLKKANRRVV--DLFEDLRDGHNLLSLLEVLSGEHLPR-EKGKMRFHMLQNAQMALDFLR 106
Cdd:cd21247    12 KLQEQRMTMQKKTFTKWMNNVFSKNGAKIEitDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 221330227  107 yKKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21247    92 -TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
154-259 1.75e-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: 1.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  154 AREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPE 233
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                          90       100
                  ....*....|....*....|....*..
gi 221330227  234 D-VDTNEPDEKSLITYISSLYDVFPEP 259
Cdd:cd21252    81 DmVSMKVPDCLSIMTYVSQYYNHFSNP 107
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
38-142 7.36e-26

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 105.50  E-value: 7.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPRE---KGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21310    16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLVS 95
                          90       100
                  ....*....|....*....|....*...
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21310    96 IDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
37-141 1.74e-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: 103.91  E-value: 1.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    37 AIQKKTFTKWVNKHLKKANRRVV--DLFEDLRDGHNLLSLLEVLSGEHLP-REKGKMRFHMLQNAQMALDFLRYK-KIKL 112
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRvtNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 221330227   113 VNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-859 1.75e-25

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 102.34  E-value: 1.75e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227   794 PLNKRRQPVNRQGPVQAICAYKQQgQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLP 859
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQG-EVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
156-256 3.11e-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: 102.93  E-value: 3.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  156 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDV 235
Cdd:cd21226     3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                          90       100
                  ....*....|....*....|.
gi 221330227  236 DTNEPDEKSLITYISSLYDVF 256
Cdd:cd21226    83 MTGNPDERSIVLYTSLFYHAF 103
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
141-256 5.12e-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: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  141 ISDIVVgkeDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIV 220
Cdd:cd21288     1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221330227  221 EKEYGVTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21288    78 EKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4334-4553 6.14e-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: 105.99  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4334 EATEFHDTLQAFVEWLTQAEKLLSNAEPVSRvLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIK 4413
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4414 NLLVSVQHRWERVVSKAAERTRALDHGYKEAREFNDAWSgMMQYLQETEQVLDQIIEEatasKEPQKIKKYIGKLKETHR 4493
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4494 QLGAKQSVYDGTMRTGKNLLERAPKGDRPVLDKMLIELKEQWTRVWSKSIDRQRKLEEAL 4553
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
153-257 6.86e-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: 102.36  E-value: 6.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   153 SAREALLRWARRSTARY-PGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK--ARNDRPRERLETAFHIVEKEYGVTR- 228
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 221330227   229 LLDPEDVdtNEPDEKSLITYISSLYDVFP 257
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
153-256 2.03e-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: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 232
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21198    80 ADmVLLSVPDKLSVMTYLHQIRAHF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3899-4111 2.49e-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: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3899 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 3978
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3979 DLDNAWDNITALYAKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMV 4058
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 4059 EVEALNRQAVELTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHAL 4111
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3571-3781 4.07e-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: 103.68  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3571 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3650
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERLEEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3651 KEIVDTVAQLCSERLGILEQALPLSEHFADSHQgLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLL 3730
Cdd:cd00176    85 NQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 3731 DKLNKTGEALGALVADDDGAKINEILDTDNARYAALRLELRERQQALESAL 3781
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
38-142 1.31e-23

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 99.39  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR---EKGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21308    20 IQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLVS 99
                          90       100
                  ....*....|....*....|....*...
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21308   100 IDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
38-142 1.60e-23

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 99.00  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPR---EKGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21309    17 IQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLVS 96
                          90       100
                  ....*....|....*....|....*...
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21309    97 IDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
41-138 3.24e-23

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: 97.00  E-value: 3.24e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227     41 KTFTKWVNKHLKKANRRVV-DLFEDLRDGHNLLSLLEVLSGEHLPREK---GKMRFHMLQNAQMALDFLRYKKIKLVNIR 116
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVtNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 221330227    117 AEDIVDGnPKLTLGLIWTIILH 138
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
153-253 3.89e-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: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|...
gi 221330227  233 ED--VDTNEPDEKSLITYISSLY 253
Cdd:cd21200    81 EDmvRMGNRPDWKCVFTYVQSLY 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4558-4766 4.70e-23

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.60  E-value: 4.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4558 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4635
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4636 EMQSIWEEVKSAVAKRGERLQVALvDAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVRER 4715
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227 4716 EKTETFEYAEDIINKAYPDAIPIIKNWLSIIQQRWEEVRQWAINRESKLEQ 4766
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
153-256 5.47e-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: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYGVTRLLDP 232
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21255    80 ADmVLLPIPDKLIVMTYLCQLRAHF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3676-3893 6.63e-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: 97.52  E-value: 6.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3676 EHFADSHQGLTAWLDDMEQQISRLSMPAlRPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3755
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3756 LDTDNARYAALRLELRERQQALESALQESSQFSDKLEgMLRALANTVDQVNQLDPLSALpQKIREQIEDNDALMDDLDKR 3835
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 3836 QDAFSAVQRAANDVIAKAGNKADPAvrdIKAKLEKLNNLWNDVQNATKKRGSSLDDIL 3893
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDADEE---IEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
158-256 3.38e-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: 91.64  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  158 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD-PEDVD 236
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|
gi 221330227  237 TNEPDEKSLITYISSLYDVF 256
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELF 108
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
150-258 4.09e-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: 91.55  E-value: 4.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  150 DNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRL 229
Cdd:cd21251     2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 221330227  230 LDPEDVDT-NEPDEKSLITYISSLYDVFPE 258
Cdd:cd21251    82 MTGKEMASvGEPDKLSMVMYLTQFYEMFKD 111
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
153-256 5.97e-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: 5.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 232
Cdd:cd21199     8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTI 86
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21199    87 DEmVSMERPDWQSVMSYVTAIYKHF 111
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
153-251 1.44e-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: 89.60  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTaryPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21184     1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
                          90       100
                  ....*....|....*....|
gi 221330227  232 PEDVDTNEPDEKSLITYISS 251
Cdd:cd21184    78 PEDMVSPNVDELSVMTYLSY 97
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
39-139 5.39e-20

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 88.02  E-value: 5.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKHLKKAN--RRVVDLFEDLRDGHNLLSLLEVLSGEHLPR--EKGKMRFHMLQNAQMALDFLRYKKIKLVN 114
Cdd:cd21212     1 EIEIYTDWANHYLEKGGhkRIITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....*
gi 221330227  115 IRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
620-796 1.44e-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: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  620 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 699
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  700 TALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFG 779
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHE 159
                         170
                  ....*....|....*..
gi 221330227  780 ETVATLQRRAQTVVPLN 796
Cdd:cd00176   160 PRLKSLNELAEELLEEG 176
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3028-3245 1.90e-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: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3028 LREFYDHQSQTLDDIQDVSDEFKRMKPVGSeLDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAI 3107
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3108 EKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAgLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKML 3187
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 3188 LDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAM 3245
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2596-2805 2.30e-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: 89.81  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2596 RHFAENCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2673
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2674 DRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWLRTAEDKLADLTPGvLSKAKLETRLRDLQTFRSEVWKHS 2753
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2754 GEFENTKGLGETFLSSCDIDKEP-IKAELQDIRDRWERLNNDLIARAHEIENC 2805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4223-4438 3.13e-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: 89.43  E-value: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4223 EAHGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIkrqNQMKVSSSN 4302
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4303 LQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDTLQaFVEWLTQAEKLLsNAEPVSRVLETIQAQMEEHKVLQKD 4382
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 4383 VSTHREAMLLLDKKGTHLKYFSQKQDVILIKNLLVSVQHRWERVVSKAAERTRALD 4438
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
156-252 3.63e-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: 85.45  E-value: 3.63e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    156 EALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKAR----NDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 221330227    232 PEDVDTNEPDEKSLITYISSL 252
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
153-253 4.21e-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: 4.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|..
gi 221330227  233 ED-VDTNEPDEKSLITYISSLY 253
Cdd:cd21259    81 EDmVRMREPDWKCVYTYIQEFY 102
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
158-256 6.50e-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: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  158 LLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLD-PEDVD 236
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|
gi 221330227  237 TNEPDEKSLITYISSLYDVF 256
Cdd:cd21250    89 AEEPDKLSMVMYLSKFYELF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4661-4833 8.87e-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: 88.27  E-value: 8.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4661 DAEKLNARVQALFDWLDHAEHKLRYAKNAPDDEKVsREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIK 4740
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4741 NWLSIIQQRWEEVRQWAINRESKLEQHLQSLKDLDDtIEELLAWLSGLEGTLLNlkhEQLPDEIPPVEKLIEDHKEFMEN 4820
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS---EDLGKDLESVEELLKKHKELEEE 154
                         170
                  ....*....|...
gi 221330227 4821 TARRQNEVDRACK 4833
Cdd:cd00176   155 LEAHEPRLKSLNE 167
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2703-2915 2.00e-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: 87.12  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2703 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2782
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2783 DIRDRWERLNNDLIARAHEIENCSRRLdDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKP 2862
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2863 LQSLKALAKDISAEARAAggDADHLTSEVDGLADRMSELQGRLDDRCGELQSA 2915
Cdd:cd00176   162 LKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
40-137 3.83e-18

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: 82.77  E-value: 3.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHLKKAN-RRVVDLFEDLRDGHNLLSLLEVLSGEHLPRE--KGKMRFHMLQNAQMALDFLR-YKKIKLVNI 115
Cdd:cd00014     1 EEELLKWINEVLGEELpVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKkLGLPELDLF 80
                          90       100
                  ....*....|....*....|...
gi 221330227  116 RAEDIV-DGNPKLTLGLIWTIIL 137
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3248-3463 5.50e-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: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3248 AKRFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGE 3327
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3328 KVRGVTERYTGLVDASDNIGALLAESRQGLRHLvLSYQDLVAWMESMEAELKRfKSVPVYAEKLLEQMDHLLELNENIAG 3407
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 3408 HASNVESTVESGAELMKHISNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAL 3463
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3141-3354 7.47e-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: 85.58  E-value: 7.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3141 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCePGERASIEKQL 3220
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3221 NDLMKRFDALTDGAEQRELDLEEAMEVAKRFHDKISpLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKK 3300
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 221330227 3301 PDFSDLADVTAQLMHLVSDEEAVNLGEKVRGVTERYTGLVDASDNIGALLAESR 3354
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
153-256 8.14e-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: 8.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKeYGVTRLLDP 232
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21254    80 SDmVLLAVPDKLTVMTYLYQIRAHF 104
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
153-256 3.51e-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: 3.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21196     3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                          90       100
                  ....*....|....*....|....
gi 221330227  233 EDVDTNEpDEKSLITYISSLYDVF 256
Cdd:cd21196    83 QAVVAGS-DPLGLIAYLSHFHSAF 105
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
153-254 7.04e-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: 7.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90       100
                  ....*....|....*....|....
gi 221330227  233 ED--VDTNEPDEKSLITYISSLYD 254
Cdd:cd21261    81 EDmmVMGRKPDPMCVFTYVQSLYN 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
153-254 8.54e-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: 8.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDP 232
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90       100
                  ....*....|....*....|....
gi 221330227  233 ED--VDTNEPDEKSLITYISSLYD 254
Cdd:cd21258    81 EDmmIMGKKPDSKCVFTYVQSLYN 104
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
146-256 8.62e-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: 8.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  146 VGKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYG 225
Cdd:cd21256     7 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVG 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221330227  226 VTRLLDPED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21256    86 IKSTLDINEmVRTERPDWQSVMTYVTAIYKYF 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1889-2098 1.27e-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: 82.11  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1889 QSQGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKK 1968
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1969 VESNLNDVTVKFEKLYEKANKRGEFLDDVYnRLSRYLDEISTVEQRMASLQEALDSRET--SLLSTEELARRMNELSRDK 2046
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLgkDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 2047 DQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAK 2098
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
155-253 1.55e-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: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  155 REALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPED 234
Cdd:cd21260     3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                          90       100
                  ....*....|....*....|
gi 221330227  235 -VDTNEPDEKSLITYISSLY 253
Cdd:cd21260    83 mVRMSVPDSKCVYTYIQELY 102
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
38-135 2.39e-16

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 77.96  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   38 IQKKTFTKWVNKHLKKAN-RRVVDLFEDLRDGHNLLSLLEVLSGEHLPRE---KGKMRFHMLQNAQMALDFLRYK-KIKL 112
Cdd:cd21225     4 VQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKIRV 83
                          90       100
                  ....*....|....*....|...
gi 221330227  113 VNIRAEDIVDGNPKLTLGLIWTI 135
Cdd:cd21225    84 QGIGAEDFVDNNKKLILGLLWTL 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3781-4002 2.62e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3781 LQESSQFSDKLEGMLRALANTVdqvnqldpLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADpa 3860
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTD--------YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3861 vrDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWkQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEI 3940
Cdd:cd00176    76 --EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 3941 RHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAM 4002
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
39-139 7.45e-16

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 76.18  E-value: 7.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKHLKK--ANRRVVDLFEDLRDGHNLLSLLEVLSGEHL------PREKGKMRfhmlQNAQMALDFLRYKKI 110
Cdd:cd21213     1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
                          90       100
                  ....*....|....*....|....*....
gi 221330227  111 KLVNIRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21213    77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
153-256 1.31e-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: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEkEYGVTRLLDP 232
Cdd:cd21257     8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                          90       100
                  ....*....|....*....|....*
gi 221330227  233 ED-VDTNEPDEKSLITYISSLYDVF 256
Cdd:cd21257    87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4443-4659 2.49e-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: 78.26  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4443 EAREFNDAWSGMMQYLQETEQVLdqiiEEATASKEPQKIKKYIGKLKETHRQLGAKQSVYDGTMRTGKNLLERAPkGDRP 4522
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL----SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4523 VLDKMLIELKEQWTRVWSKSIDRQRKLEEALLLSGQFSDALgELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQ 4602
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4603 DLQKRAAQMQGVLKTGRDLERSGNN---PEVGRQLDEMQSIWEEVKSAVAKRGERLQVAL 4659
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPdadEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3465-3672 6.95e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3465 LVQQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIES 3535
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSstdyGDDLESVEALlkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3536 IVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgDIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISS 3615
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227 3616 QKGRVRDVTAASKKvLRESPQSENTATLREKLDDLKEIVDTVAQLCSERLGILEQAL 3672
Cdd:cd00176   158 HEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4116-4218 1.02e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 72.75  E-value: 1.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4116 QFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIetEKGSVEASTTQEK 4195
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 221330227   4196 LRKLNNEWKQLLQKASDRQHELE 4218
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2808-3025 1.25e-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: 76.33  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2808 RLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAaggDADHL 2887
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP---DAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2888 TSEVDGLADRMSELQGRLDDRCGELQSAAtAVSQFNEQMKSLGIDLNDLETEIEKlSPPGREIKIVQVQIDDVGKIQTKL 2967
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 2968 DRLVGRLEDAERAADVLVDAGFAADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTL 3025
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2378-2592 2.66e-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: 75.17  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2378 KLRDFLDTHGNLKSWLDSKERMLTVLGPISsDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAV 2457
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2458 EIKLKDILGKWDDLVGKLDDRANSLGGAADSSKEFDAAVnRLREALQNISDNLDTLPTDGDH---QENLRKIENLERQLE 2534
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLesvEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 2535 GQRPLLADVEQSAATLCNiLGDPASRADVNSRVAALEKQYLALQKKLDTKKAETEASL 2592
Cdd:cd00176   157 AHEPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
524-713 4.84e-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: 74.40  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  524 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 600
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVeaLNELGEQLIEEGHPDAEEiQERLEELN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  601 KVYAELLSTSTKRLSDLD---SLQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATI 677
Cdd:cd00176    86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 221330227  678 LDRGEALLNQQHPAS-KCIEAHLTALQQQWAWLLQLT 713
Cdd:cd00176   166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
153-258 5.33e-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: 70.87  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21230     1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90       100
                  ....*....|....*....|....*..
gi 221330227  232 PEDVDTNEPDEKSLITYISSlydvFPE 258
Cdd:cd21230    78 PEEIINPNVDEMSVMTYLSQ----FPK 100
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
41-142 1.85e-13

third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409147  Cd Length: 117  Bit Score: 69.96  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   41 KTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLEVL-------SGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLV 113
Cdd:cd21298     9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
                          90       100
                  ....*....|....*....|....*....
gi 221330227  114 NIRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21298    87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4112-4219 8.31e-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: 67.73  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4112 LHLGQFQHALNELLVWINKTDSTLDQlKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIEteKGSVEAST 4191
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 221330227  4192 TQEKLRKLNNEWKQLLQKASDRQHELEE 4219
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4007-4108 1.13e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.97  E-value: 1.13e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4007 EFHETLQNLLKFLTKAEDKFAHLGaVGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTERtSPEQAASIREPL 4086
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   4087 SVVNRRWEALLRGMVERQKQLE 4108
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
34-133 1.36e-12

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 67.45  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAiqkKTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLE-VLSGE-------HLPREKGKMRFHMLQNAQMALDFL 105
Cdd:cd21300     6 EREA---RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
                          90       100
                  ....*....|....*....|....*...
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIW 133
Cdd:cd21300    81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
SPEC smart00150
Spectrin repeats;
4558-4656 2.01e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 2.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4558 QFSDALGELLDWLKKAKSRLnENGPVHGDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSG--NNPEVGRQLD 4635
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   4636 EMQSIWEEVKSAVAKRGERLQ 4656
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
40-139 3.02e-12

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409071  Cd Length: 121  Bit Score: 66.46  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLP----REKGKMRFHMLQNAQMALDFLRYKKIKLVNI 115
Cdd:cd21222    18 KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPKI 97
                          90       100
                  ....*....|....*....|....
gi 221330227  116 RAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21222    98 RPEDIVNGDLKSILRVLYSLFSKY 121
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
152-250 4.27e-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: 4.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  152 VSAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLL 230
Cdd:cd21229     2 IPPKKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVL 78
                          90       100
                  ....*....|....*....|
gi 221330227  231 DPEDVDTNEPDEKSLITYIS 250
Cdd:cd21229    79 SPEDLSSPHLDELSGMTYLS 98
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
32-138 4.95e-12

third 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. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein 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, which 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 65.77  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDaiqKKTFTKWVNKHLkkANRRVVDLFEDLRDGHNLLSLLE-----VLSGEHLPREKGKMRFHMLQNAQMALDFLR 106
Cdd:cd21219     1 EGSRE---ERAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKPLNKFKKVENCNYAVDLAK 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221330227  107 YKKIKLVNIRAEDIVDGNPKLTLGLIWTIILH 138
Cdd:cd21219    76 KLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
155-254 4.97e-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: 65.44  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  155 REALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARN---DRPRERLETAFHIVEKE-YGVTRLL 230
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkspFKKRENINLFLNACKKLgLPELDLF 80
                          90       100
                  ....*....|....*....|....
gi 221330227  231 DPEDVdTNEPDEKSLITYISSLYD 254
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
40-136 2.80e-11

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 63.36  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHL-KKANRRVV--------DLFEDLRDGHNLLSLLE-VLSG----EHLPREKGKMRFHMLQNAQMALDFL 105
Cdd:cd21217     3 KEAFVEHINSLLaDDPDLKHLlpidpdgdDLFEALRDGVLLCKLINkIVPGtideRKLNKKKPKNIFEATENLNLALNAA 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIWTII 136
Cdd:cd21217    83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
45-135 5.22e-11

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: 62.70  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   45 KWVNKHLKKANR---RVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKM---RFHMLQNAQMALDFLRykKIKLVN-IRA 117
Cdd:cd21218    17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
                          90
                  ....*....|....*...
gi 221330227  118 EDIVDGNPKLTLGLIWTI 135
Cdd:cd21218    95 EDIVSGNPRLNLAFVATL 112
SPEC smart00150
Spectrin repeats;
621-721 1.41e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 1.41e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    621 QHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHLT 700
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227    701 ALQQQWAWLLQLTLCLEVHLK 721
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1774-1998 2.67e-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: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1774 RQREYQDALDKANEWLRSVHPRVSriiSEPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLrslggQLSPM 1853
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS---STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-----EEGHP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1854 EINQLELPIADLKNNYQQLLDNLGEHCKTLDKTLVQSQGVQDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHK 1933
Cdd:cd00176    73 DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDL--ESVEELLKKHK 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221330227 1934 VLLADLQSHQASIDSVQVSAKHLLASASNARiAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVY 1998
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDA-DEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1083-1320 3.44e-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: 63.23  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1083 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1162
Cdd:cd00176     9 ADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1163 RLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVeESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENvnva 1242
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA---- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227 1243 ggrliREAKIydSKCLRFVDWLVEARPsfspprrdlrpadsdPGATQYYSQRLDNLNTKNDRLLEQLSQRLKTAIEVN 1320
Cdd:cd00176   158 -----HEPRL--KSLNELAEELLEEGH---------------PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
4225-4329 3.67e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 3.67e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4225 HGYIAEVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIKRQNQmkvSSSNLQ 4304
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP---DAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   4305 HTLRTLKQRWDAVVSRASDKKIKLE 4329
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3541-4225 4.62e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 4.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3541 NRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADlpamepKLVRAQLQEHRSINDDISSQKGRV 3620
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ------KELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3621 RDVTAASKKV---LRESPQS-----ENTATLREKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDM 3692
Cdd:TIGR02168  312 ANLERQLEELeaqLEELESKldelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3693 EQQISRLSMPALRPD-QITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALvaDDDGAKINEILDTDNARYAALRLE 3769
Cdd:TIGR02168  392 ELQIASLNNEIERLEaRLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3770 LRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPLSAL---PQKIREQIED------ND 3826
Cdd:TIGR02168  470 LEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVLSELisvDEGYEAAIEAalggrlQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3827 ALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA---------------VRDIKAKLEKLNNLW-------N 3876
Cdd:TIGR02168  550 VVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvakdLVKFDPKLRKALSYLlggvlvvD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3877 DVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEETLscqeppAAQPQDIKKQQVALQEI 3940
Cdd:TIGR02168  630 DLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEKI------EELEEKIAELEKALAEL 703
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3941 RHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLQNLLKFLT 4020
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4021 KAEDKFAHLGAvgsDIDAVKRQIEQLKSfkdevdphmvEVEALNRQAVELTERtspeqAASIREPLSVVNRRWEALLRGM 4100
Cdd:TIGR02168  779 EAEAEIEELEA---QIEQLKEELKALRE----------ALDELRAELTLLNEE-----AANLRERLESLERRIAATERRL 840
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4101 VERQKQLEHALLHLGQFQHALNELLVWINKtdstldqlkpipgdpqlLEVELAKLKVLANDIQAHQNSV-DTLNDAGRQL 4179
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEE-----------------LESELEALLNERASLEEALALLrSELEELSEEL 903
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*.
gi 221330227  4180 IETEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALREAH 4225
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
SPEC smart00150
Spectrin repeats;
4337-4438 7.19e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 7.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4337 EFHDTLQAFVEWLTQAEKLLSnAEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKyFSQKQDVILIKNLL 4416
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   4417 VSVQHRWERVVSKAAERTRALD 4438
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
5230-5367 7.80e-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: 7.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5230 SKPPSRHGSTLSLDSTDDhtPSRIPQRKPSTGSTASGTTPRPARLSVTTTTTPGSRLNGTStitrKTASGSASPAPTSNg 5309
Cdd:pfam09595   33 LILIGESNKEAALIITDI--IDININKQHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNN----QHPSQDRSEAPPLE- 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227  5310 gmSRSSSIPALTgfgfkpiRRNiSGSSTPSGMQTPRKSSAEPTFSSTMRRTSRGTTPT 5367
Cdd:pfam09595  106 --PAAKTKPSEH-------EPA-NPPDASNRLSPPDASTAAIREARTFRKPSTGKRNN 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2771-3296 9.32e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2771 DIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDpkLLERVK 2850
Cdd:PRK02224  191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED--LRETIA 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2851 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 2930
Cdd:PRK02224  269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2931 IDLNDLETEIEKLSPPGREI-KIVQVQIDDVGKIQTKLDRLVGRLEDAERAADvlvdagfaaDTTQTREQISTLRKTLGR 3009
Cdd:PRK02224  349 EDADDLEERAEELREEAAELeSELEEAREAVEDRREEIEELEEEIEELRERFG---------DAPVDLGNAEDFLEELRE 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3010 LDNRVRDHEDNLHSTLKALREFYDHQSQTLDD------IQDVSDEfkrmkPVGSELDQIRRQQEDFrnfrERKVEPLAIN 3083
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGS-----PHVETIEEDRERVEEL----EAELEDLEEE 490
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3084 VDKVNvagrDLVRSAGSGVSTtaiEKDLEKLNDRWNDLKERMNERDRRLDvallqsgKFQEALAGLSKWLSDTE-EMVAN 3162
Cdd:PRK02224  491 VEEVE----ERLERAEDLVEA---EDRIERLEERREDLEELIAERRETIE-------EKRERAEELRERAAELEaEAEEK 556
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3163 QKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVAnhcepgERASIEKQLNDLMKRFDALTDGAEQRELDLE 3242
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA------AIADAEDEIERLREKREALAELNDERRERLA 630
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 3243 EAMEVAKRFHDKISP--LELWLDNTERSVKAMELIptdEEKIQQRIREHDRLHDEI 3296
Cdd:PRK02224  631 EKRERKRELEAEFDEarIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEI 683
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
39-138 1.15e-09

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which 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. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409148  Cd Length: 114  Bit Score: 59.05  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLE-----VLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLV 113
Cdd:cd21299     5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLV 82
                          90       100
                  ....*....|....*....|....*
gi 221330227  114 NIRAEDIVDGNPKLTLGLIWTIILH 138
Cdd:cd21299    83 NVAGNDIVQGNKKLILALLWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2490-2698 1.19e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.69  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2490 KEFDAAVNRLREALQNISDnLDTLPTDGDHQENLRKIENLERQLEGQRPLLADVEQSAATLCNilGDPASRADVNSRVAA 2569
Cdd:cd00176     7 RDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2570 LEKQYLALQKKLDTKKAETEASLRDGRHFAEnCSKTLGWLGGELSNLTDRLLVSaHKPTLQHQIDTHEPIYREVMAREHE 2649
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 2650 VIMLINKGKDLTDRQQDRG---VKRDLDRIQQQWEKLRREAVDRHTRLQTCM 2698
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAdeeIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
156-252 1.63e-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: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  156 EALLRWARRSTARYpGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRK----------------------------ARND 207
Cdd:cd21224     3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAirqpttqtvdraqdeaedfwvaefspstGDSG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227  208 RPRERLETA---FHIVEKEY----GVTRLLDPEDVDTNEPDEKSLITYISSL 252
Cdd:cd21224    82 LSSELLANEkrnFKLVQQAVaelgGVPALLRASDMSNTIPDEKVVILFLSYL 133
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5120-5365 3.34e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.04  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5120 STPNAAATASSSPHAHNGGSSN---LPPYMSGQGPIIKVRERSVRSIP-----MSRPSRSSLSASTPDSLSDNEGSHGGP 5191
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPpaaASPRPPRRSSPISASASSPAPAPgrsaaDDAGASSSDSSSSESSGCGWGPENECP 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5192 SGRYTPrKVTYTSTRTGLTPG--GSRAGSKPNSRPLSRQGSKPPSRHGSTLSLDSTDDHTPSRIPQRKPSTGST------ 5263
Cdd:PHA03307  257 LPRPAP-ITLPTRIWEASGWNgpSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTsssses 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5264 ----ASGTTPRPARLSvtTTTTPGSRLNGTSTITRKTASGSASPAPTSNGGMSRSSSIPALTGFGfkpiRRNISGSSTPS 5339
Cdd:PHA03307  336 srgaAVSPGPSPSRSP--SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRA----RRRDATGRFPA 409
                         250       260
                  ....*....|....*....|....*.
gi 221330227 5340 GMQTPRKSSAEPTFSSTMRRTSRGTT 5365
Cdd:PHA03307  410 GRPRPSPLDAGAASGAFYARYPLLTP 435
SPEC smart00150
Spectrin repeats;
4663-4765 6.36e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.57  E-value: 6.36e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4663 EKLNARVQALFDWLDHAEHKLRyAKNAPDDEKVSREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIKNW 4742
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDA-EEIEER 78
                            90       100
                    ....*....|....*....|...
gi 221330227   4743 LSIIQQRWEEVRQWAINRESKLE 4765
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
29-135 8.06e-09

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 56.90  E-value: 8.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   29 LRIADERDAIQKKTFTKWVNKHLKKA--NRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKG--KMRFHMLQNAQMALDF 104
Cdd:cd21285     1 GKSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  105 LRYKKIKLVNIRAEDIVDGNPKLTLGLIWTI 135
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
57-136 1.04e-08

first 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 the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 56.06  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   57 RVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKM----RFHMLQNAQMALDFLR----YKKIKLVNIRAEDIVDGNPKLT 128
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKeagvLRGGDGGGITAKDIVDGHREKT 104

                  ....*...
gi 221330227  129 LGLIWTII 136
Cdd:cd21223   105 LALLWRII 112
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2847-3611 1.54e-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: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2847 ERVKAIREELTNLSKPL---------QSLKALAKDISAEAR---AAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQS 2914
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrleelrEELEELQEELKEAEEeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2915 AATAVS-------QFNEQMKSLGIDLNDLETEIEK-----------LSPPGREIKIVQVQIDDVGKIQTKLDRLVGRLED 2976
Cdd:TIGR02168  293 LANEISrleqqkqILRERLANLERQLEELEAQLEEleskldelaeeLAELEEKLEELKEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2977 AERAADVLVDAgFAADTTQTREQISTLRKTLGRLDNRVRDHEDNlhstlkalrefydhQSQTLDDIQDVSDEFKR--MKP 3054
Cdd:TIGR02168  373 RLEELEEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEaeLKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3055 VGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAGRDLVrsagsgvsttAIEKDLEKLNDRWNDLkERMNERDRRLDV 3134
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----------AAERELAQLQARLDSL-ERLQENLEGFSE 506
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3135 ALLQSGKFQEALAGLSKWLSDT-------EEMVANQKPPSSDYKVVK---AQLQEQKFLKK--------MLLDRQNSMGS 3196
Cdd:TIGR02168  507 GVKALLKNQSGLSGILGVLSELisvdegyEAAIEAALGGRLQAVVVEnlnAAKKAIAFLKQnelgrvtfLPLDSIKGTEI 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3197 LANLGKEVANH-CEPGERASIEKQLNDLMKRFDALTDG---AEqrelDLEEAMEVAKrfhdKISPLELWLdntersVKAM 3272
Cdd:TIGR02168  587 QGNDREILKNIeGFLGVAKDLVKFDPKLRKALSYLLGGvlvVD----DLDNALELAK----KLRPGYRIV------TLDG 652
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3273 ELIPTD----------EEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKVRGVTERYTGLVDA 3342
Cdd:TIGR02168  653 DLVRPGgvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISAL 731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3343 SDNIGALLAESRQGLRHLVLSYQDLVAWMESMEAELKRFKSVpvyAEKLLEQMDHLLELNENIAGHASNVESTVESGAEL 3422
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3423 mkhisNDEAIQLKDKLDSLQRRYGDLTNRGGDLLKSAQNAlplvqqfHEAHNRLVEWMQSAEAALAPSEPRQAdvlRLEG 3502
Cdd:TIGR02168  809 -----RAELTLLNEEAANLRERLESLERRIAATERRLEDL-------EEQIEELSEDIESLAAEIEELEELIE---ELES 873
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3503 ELADMRPILDSINQvGPQLCQLSPGEGAATIESIvtrdNRRFDSIVEQIQRKAERLHLSNQRAKEVTGDIDELLEWFREm 3582
Cdd:TIGR02168  874 ELEALLNERASLEE-ALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE- 947
                          810       820
                   ....*....|....*....|....*....
gi 221330227  3583 DTTLREADLPAMEPKLVRAQLQEHRSIND 3611
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3106-3846 1.74e-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: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3106 AIEKDLEKLNDRWNDLKERMNERDRRLDVAllqsgkfQEALAGLSKWLSDTEEMV--ANQKPPSSDYKVVKAQLQEQKFL 3183
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEEL-------QKELYALANEISRLEQQKqiLRERLANLERQLEELEAQLEELE 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3184 KKMLLDRQNsmgsLANLGKEVAnhcepgeraSIEKQLNDL---MKRFDALTDGAEQRELDLEEAMEvakRFHDKISPLEL 3260
Cdd:TIGR02168  330 SKLDELAEE----LAELEEKLE---------ELKEELESLeaeLEELEAELEELESRLEELEEQLE---TLRSKVAQLEL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3261 WLDNTERSVKAMeliptdEEKIQQRIREHDRLHDEI--LGKKPDFSDLADVTAQLMHLvsDEEAVNLGEKVRGVTERYtg 3338
Cdd:TIGR02168  394 QIASLNNEIERL------EARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEEL--EEELEELQEELERLEEAL-- 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3339 lvdasDNIGALLAESRQGLRHLVLSYQDLVAWMESMEAELKRFKSvpvYAEKLLEQMDHLLELNeNIAGHAS---NVEST 3415
Cdd:TIGR02168  464 -----EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGLS-GILGVLSeliSVDEG 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3416 VES------GAELMKHISNDEAIQLKDkLDSL-QRRYGDLT------NRGGDLLKSAQNALPLVQQFHEAHNRLVEWMQS 3482
Cdd:TIGR02168  535 YEAaieaalGGRLQAVVVENLNAAKKA-IAFLkQNELGRVTflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3483 AEAALAPSEPRQADVLRLEGELADMRPILDSINQVGPQLCQLSP-----GEGAATIESIVTRDNRRfDSIVEQIQRKAER 3557
Cdd:TIGR02168  614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvitGGSAKTNSSILERRREI-EELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3558 LHLSNQRAKEVTGDIDELLEWFREMDTTLREA--DLPAMEPKLVRAQlQEHRSINDDISSQKGRVRDVTAASKKVLRESP 3635
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELsrQISALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3636 QS-ENTATLREKLDDLKEIVDTVAQLCS---ERLGILEQALP-LSEHFADSHQGLTAWLDDMEQQISRLSMPALRPDQIT 3710
Cdd:TIGR02168  772 EAeEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3711 LQQdknERLLQSIAEHKPLLDKLNKTGEALGALVadddgAKINEILDTDNARYAALRLELRE---RQQALESALQES--- 3784
Cdd:TIGR02168  852 EDI---ESLAAEIEELEELIEELESELEALLNER-----ASLEEALALLRSELEELSEELRElesKRSELRRELEELrek 923
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221330227  3785 -SQFSDKLEGMLRALANTVDQVNQ-----LDPLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAA 3846
Cdd:TIGR02168  924 lAQLELRLEGLEVRIDNLQERLSEeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
41-135 2.03e-08

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 55.04  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   41 KTFTKWVNKHLKKAN--RRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKG--KMRFHMLQNAQMALDFLRYKKIKLVNIR 116
Cdd:cd21286     3 KIYTDWANHYLAKSGhkRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLS 82
                          90
                  ....*....|....*....
gi 221330227  117 AEDIVDGNPKLTLGLIWTI 135
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSL 101
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
153-258 2.31e-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: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21314    11 TPKQRLLGWIQN---KVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                          90       100
                  ....*....|....*....|....*..
gi 221330227  232 PEDVDTNEPDEKSLITYISSlydvFPE 258
Cdd:cd21314    88 PEEIVDPNVDEHSVMTYLSQ----FPK 110
SPEC smart00150
Spectrin repeats;
3676-3778 5.37e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 5.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3676 EHFADSHQGLTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALvADDDGAKINEI 3755
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 221330227   3756 LDTDNARYAALRLELRERQQALE 3778
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3141-3242 6.78e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 6.78e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3141 KFQEALAGLSKWLSDTEEMVAnQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPgERASIEKQL 3220
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   3221 NDLMKRFDALTDGAEQRELDLE 3242
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3899-3998 9.08e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 9.08e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3899 FWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMcGEPDKPEVKKHIE 3978
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 221330227   3979 DLDNAWDNITALYAKREENL 3998
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3434-4274 9.95e-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: 58.91  E-value: 9.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3434 LKDKLDSLQR------RYGDLTNRggdlLKSAQNALpLVQQFHEAHNRLVEWMQSAEAALAPSEPRQADVLRLEGELADM 3507
Cdd:TIGR02168  198 LERQLKSLERqaekaeRYKELKAE----LRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3508 RPILDSINqvgpqlcqlspgEGAATIESIVTRDNRRFDSIVEQIQRKAERLHLSNQRAKEVTgdiDELLEWFREMDTTlr 3587
Cdd:TIGR02168  273 RLEVSELE------------EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDEL-- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3588 EADLPAMEPKLvrAQLQEhrsinddissqkgrvrDVTAASKKVLRESPQSENtatLREKLDDLKEIVDTVAqlcSERLGI 3667
Cdd:TIGR02168  336 AEELAELEEKL--EELKE----------------ELESLEAELEELEAELEE---LESRLEELEEQLETLR---SKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3668 LEQALPLSEhfadshqgltawlddmeqQISRLSmpalrpDQITLQQDKNERLLQSIAEH--KPLLDKLNKTGEALGALva 3745
Cdd:TIGR02168  392 ELQIASLNN------------------EIERLE------ARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEEL-- 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3746 DDDGAKINEILDTDNARYAALRLELRERQQALESA---LQESSQFSDKLEGMLRALANTVDQVNQL-----------DPL 3811
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilGVL 525
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3812 SAL---PQKIREQIED------NDALMDDLDKRQDAFSAVQRAAN--------DVIAKAGNKADPA-------------- 3860
Cdd:TIGR02168  526 SELisvDEGYEAAIEAalggrlQAVVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGNDReilkniegflgvak 605
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3861 -VRDIKAKLEKLNNLW-------NDVQNATKKRGS--------SLDDIL-----SVAEPFWKQLNSVMKT---LKDLEET 3916
Cdd:TIGR02168  606 dLVKFDPKLRKALSYLlggvlvvDDLDNALELAKKlrpgyrivTLDGDLvrpggVITGGSAKTNSSILERrreIEELEEK 685
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3917 LscqeppAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKKHIEDLDNAWDNITALYAKREE 3996
Cdd:TIGR02168  686 I------EELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3997 NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAHLGAvgsDIDAVKRQIEQLKSfkdevdphmvEVEALNRQAVELTERtsp 4076
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEA---QIEQLKEELKALRE----------ALDELRAELTLLNEE--- 818
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4077 eqAASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALNELLVWINKTDSTLDQL-KPIPGDPQLLEVELAKL 4155
Cdd:TIGR02168  819 --AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEEALALLRSEL 896
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4156 KVLANDIQAHQNSVDTLNdagRQLIETEKGSVEASTTQEKLR--------KLNNEWKQLLQKASDRQHELEEALREAHGY 4227
Cdd:TIGR02168  897 EELSEELRELESKRSELR---RELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRR 973
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|....*..
gi 221330227  4228 IAEVQDILGWLGDVDavigaskpvgglpETATEQLERFMEVYNELDE 4274
Cdd:TIGR02168  974 LKRLENKIKELGPVN-------------LAAIEEYEELKERYDFLTA 1007
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
401-619 1.06e-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: 55.91  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  401 HVDQKLTDLEGRIGEEGRRIERLHPVDAKSIVE-------ALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNK 473
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEallkkheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  474 LHQRWAQLRtnfhtnlvqklsglkypvhETTVTRQTRMVVESRQidtNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSV 553
Cdd:cd00176    84 LNQRWEELR-------------------ELAEERRQRLEEALDL---QQFFRDADDLEQWLEEKEAALASEDLGKDLESV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  554 KEELDRQQHEHKIIDQFHTKILNDERQQTKF----SGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDS 619
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
151-258 1.21e-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: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  151 NVSAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRL 229
Cdd:cd21313     6 KQTPKQRLLGWIQN---KIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQV 82
                          90       100
                  ....*....|....*....|....*....
gi 221330227  230 LDPEDVDTNEPDEKSLITYISSlydvFPE 258
Cdd:cd21313    83 ITPEEIIHPDVDEHSVMTYLSQ----FPK 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
977-1180 2.00e-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: 55.14  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  977 FTEECLAIKSKLEDMARELDQiilAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALK----TPVLKKSL 1052
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1053 DNLMELWKELNTQSglhKDRLKLLEASLAGLEDNEHV------ISELENELARhQDLPSTAEGLQQVFKQLNHMQDIITQ 1126
Cdd:cd00176    82 EELNQRWEELRELA---EERRQRLEEALDLQQFFRDAddleqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 221330227 1127 QQPQMDKMNDAADQLGRMGVPTKVLGDLKRLhsnvERLNTRWSAVCNQLGERMR 1180
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL----EELNERWEELLELAEERQK 207
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5111-5318 2.30e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.87  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5111 SMAAFTPRRSTPNAAATASSSPHAHNGGSSNLPPYMSGQGPIIKVRERSVRSIPMSRPSRSSLSASTPDSLSDNEGSHGG 5190
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5191 PSGRYTPRkvtytstrtglTPGGSRAGSKPNSRPLSR-QGSKPPSRHGSTLSLDSTDDH---TPSRIPQRKPSTGSTASG 5266
Cdd:PHA03307  291 PRERSPSP-----------SPSSPGSGPAPSSPRASSsSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSRPPPP 359
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5267 TTP-------RPARLSVTTTTTPGSrlnGTSTITRKTASGSASPAPTSN-GGMSRSSSIP 5318
Cdd:PHA03307  360 ADPssprkrpRPSRAPSSPAASAGR---PTRRRARAAVAGRARRRDATGrFPAGRPRPSP 416
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
620-713 3.20e-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: 51.55  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   620 LQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHL 699
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 221330227   700 TALQQQWAWLLQLT 713
Cdd:pfam00435   83 EELNERWEQLLELA 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2458-3296 3.23e-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: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2458 EIKLKDILGKWDDLVGKLDDRANSLGGAADS-------SKEFDAAVNRLREALQNISDNLDTLptDGDHQENLRKIENLE 2530
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEEleeltaeLQELEEKLEELRLEVSELEEEIEEL--QKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2531 RQLEGQRPLLADVEQSAATLCNILGDPASRAD-VNSRVAALEKQYLALQKKLDTKKAETEAslrdgrhfaencsktlgwL 2609
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEELESLEAELEE------------------L 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2610 GGELSNLTDRLLvsahkpTLQHQIDTHEP----IYREVMAREHEVIMLINKGKDLTDRQQ----------DRGVKRDLDR 2675
Cdd:TIGR02168  364 EAELEELESRLE------ELEEQLETLRSkvaqLELQIASLNNEIERLEARLERLEDRRErlqqeieellKKLEEAELKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2676 IQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRDLQTFRSEVWKHSGE 2755
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2756 FENTKGLgetflsscdidkepiKAELQDIRDRWER-LNNDLIARAHEIenCSRRLDDFNDELRNL-DHSLGRCEdrLAAH 2833
Cdd:TIGR02168  518 LSGILGV---------------LSELISVDEGYEAaIEAALGGRLQAV--VVENLNAAKKAIAFLkQNELGRVT--FLPL 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2834 DALGGAAKDPKLLERvkaireeLTNLSKPLQSLKALAKdISAEARAAGGDADHLTSEVDGLADRMsELQGRLDDRC---- 2909
Cdd:TIGR02168  579 DSIKGTEIQGNDREI-------LKNIEGFLGVAKDLVK-FDPKLRKALSYLLGGVLVVDDLDNAL-ELAKKLRPGYrivt 649
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2910 --GELQSAATAVSQfneqmKSLGIDLNDLET--EIEKLSppgREIKIVQVQIDDvgkIQTKLDRLVGRLEDAERAADVLV 2985
Cdd:TIGR02168  650 ldGDLVRPGGVITG-----GSAKTNSSILERrrEIEELE---EKIEELEEKIAE---LEKALAELRKELEELEEELEQLR 718
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2986 dagfaADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKpvgselDQIRRQ 3065
Cdd:TIGR02168  719 -----KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEEL 787
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3066 QEDFRNFRERkveplainvdkvnvagrdlvrsagsgvsTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEA 3145
Cdd:TIGR02168  788 EAQIEQLKEE----------------------------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3146 LAGLSKWLSDTEEMVANQKPPSSDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcepgERASIEKQLNDLMK 3225
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE----ELRELESKRSELRR 915
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221330227  3226 RFDALTDGAEQRELDLEEAMEVAKRFHDKISplELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEI 3296
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2238-3010 4.68e-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: 56.60  E-value: 4.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2238 SELSPVQQQLSEinnrygligvrLNDRQHELDNLNEELRKQYENLKGLAQFLE-RIQRQlpkesVSNKDEAERCIKQARK 2316
Cdd:TIGR02168  260 AELQELEEKLEE-----------LRLEVSELEEEIEELQKELYALANEISRLEqQKQIL-----RERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2317 ILEDMYEKQSLLDTTKAQVKDILrrksdvpgaEQLRQENDSIQEKWKNLNDICKNRIAFSEKLRDFLDThgnLKSWLDSK 2396
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKL---------EELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2397 ERMLTVL-GPISS-DPRMVQSQVQQVQVLRE-EFRTQQPQLKHFQELGHDVVDHLAGTPDAQAVEIKLKDILGKWDDLVG 2473
Cdd:TIGR02168  392 ELQIASLnNEIERlEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2474 KLDDRANSLggaadsSKEFDAAVNRLrEALQNISDNLDTLptdgdhQENLRKIENLERQLEGQRPLLAD---VEQS---- 2546
Cdd:TIGR02168  472 EAEQALDAA------ERELAQLQARL-DSLERLQENLEGF------SEGVKALLKNQSGLSGILGVLSElisVDEGyeaa 538
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2547 -AATLCNILGDPASR--ADVNSRVAALEKQ------YLALQ----KKLDTKKAETEASLRDGRHFAENCSKTLGWLGGEL 2613
Cdd:TIGR02168  539 iEAALGGRLQAVVVEnlNAAKKAIAFLKQNelgrvtFLPLDsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2614 SNLTDRLLVSAHKPTLQHQIDTHEPIYREVMArEHEVIM---LINKGKDLTDrQQDRGVKRDLDRIQQQWEKLRREAVDR 2690
Cdd:TIGR02168  619 SYLLGGVLVVDDLDNALELAKKLRPGYRIVTL-DGDLVRpggVITGGSAKTN-SSILERRREIEELEEKIEELEEKIAEL 696
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2691 HTRLQTcmehCKKYSQTSETFLAWLRTA-EDKLADLTPGVLSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETflss 2769
Cdd:TIGR02168  697 EKALAE----LRKELEELEEELEQLRKElEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE---- 768
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2770 cdiDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKD--PKLLE 2847
Cdd:TIGR02168  769 ---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERrlEDLEE 845
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2848 RVKAIREELTNLSKPLQSLKALAKDISAEaraaggdADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMK 2927
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2928 SLGIDLNDLETEIEKLSppgreikivqvqiddvGKIQTKLDRLVGRLEDAERAADVLVdAGFAADTTQTREQISTLRKTL 3007
Cdd:TIGR02168  919 ELREKLAQLELRLEGLE----------------VRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKI 981

                   ...
gi 221330227  3008 GRL 3010
Cdd:TIGR02168  982 KEL 984
SPEC smart00150
Spectrin repeats;
3571-3669 5.04e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 5.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3571 DIDELLEWFREMDTTLREADLPAmEPKLVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPqsENTATLREKLDDL 3650
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEERLEEL 82
                            90
                    ....*....|....*....
gi 221330227   3651 KEIVDTVAQLCSERLGILE 3669
Cdd:smart00150   83 NERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3250-3350 6.62e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 6.62e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3250 RFHDKISPLELWLDNTERSVKAMElIPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLvSDEEAVNLGEKV 3329
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   3330 RGVTERYTGLVDASDNIGALL 3350
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
289-615 8.42e-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: 8.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   289 REKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYFETVGEVDVEAELrpdaiekawyrmn 368
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------- 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   369 taLQDREvilQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEGRRIERLhpvdaKSIVEALETEIRHleEPIQD 448
Cdd:TIGR02169  728 --LEQEE---EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-----EEALNDLEARLSH--SRIPE 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   449 MNQ------DCHVLNEGRyphVSELHKKVNKLHQRWAQLRtnfhtnlvQKLSGLKYPVHETTVTRQTRmvvESRQIDTNP 522
Cdd:TIGR02169  796 IQAelskleEEVSRIEAR---LREIEQKLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSI---EKEIENLNG 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   523 HFRDLQEHIEWCQNKLKQLlaADYGSDLPSVKEELDRQQHEHKI-IDQFHTKIlNDERQQTKFSGDELALYQQRLNQLQK 601
Cdd:TIGR02169  862 KKEELEEELEELEAALRDL--ESRLGDLKKERDELEAQLRELERkIEELEAQI-EKKRKRLSELKAKLEALEEELSEIED 938
                          330
                   ....*....|....
gi 221330227   602 VYAELLSTSTKRLS 615
Cdd:TIGR02169  939 PKGEDEEIPEEELS 952
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2845-3075 9.60e-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: 9.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2845 LLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVD--GLADRMSELQGRLDdrcgELQSAATAVSQF 2922
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELE----RLDASSDDLAAL 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2923 NEQMKSLGIDLNDLETEIEKLSppgREIKIVQVQIDDvgkIQTKLDRLVGRLEDAERAADVLVDAGF------AADTTQT 2996
Cdd:COG4913   691 EEQLEELEAELEELEEELDELK---GEIGRLEKELEQ---AEEELDELQDRLEAAEDLARLELRALLeerfaaALGDAVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2997 REQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLD-DIQDVsDEFKRMkpvgseLDQIR-----RQQEDFR 3070
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDaDLESL-PEYLAL------LDRLEedglpEYEERFK 837

                  ....*
gi 221330227 3071 NFRER 3075
Cdd:COG4913   838 ELLNE 842
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2778-3053 9.64e-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: 9.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2778 KAELQDIRDRWERLNNDLIARAHEIEN-------CSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVK 2850
Cdd:TIGR02169  715 SRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2851 AIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMK--- 2927
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEele 874
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2928 ----SLGIDLNDLETEIEKLSPPGREIKIVQVQIDdvGKIQTKLDRLVGRLEDAERAADVL--VDAGFAADTTQTREQIS 3001
Cdd:TIGR02169  875 aalrDLESRLGDLKKERDELEAQLRELERKIEELE--AQIEKKRKRLSELKAKLEALEEELseIEDPKGEDEEIPEEELS 952
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221330227  3002 --TLRKTLGRLDNRVRDHED-NL------HSTLKALREfYDHQSQTL----DDIQDVSDEFKRMK 3053
Cdd:TIGR02169  953 leDVQAELQRVEEEIRALEPvNMlaiqeyEEVLKRLDE-LKEKRAKLeeerKAILERIEEYEKKK 1016
SPEC smart00150
Spectrin repeats;
2703-2803 1.11e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   2703 KYSQTSETFLAWLRTAEDKLADLTPGVlSKAKLETRLRDLQTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIKAELQ 2782
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   2783 DIRDRWERLNNDLIARAHEIE 2803
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
153-250 1.21e-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: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARrstARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21315    16 TPKQRLLGWIQ---SKVPDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
                          90
                  ....*....|....*....
gi 221330227  232 PEDVDTNEPDEKSLITYIS 250
Cdd:cd21315    93 PEEMVNPKVDELSMMTYLS 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2773-3083 1.41e-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: 55.06  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2773 DKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAahdalggaakdpKLLERVKAI 2852
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE------------EAEEELAEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2853 REELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGID 2932
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2933 LNDLETEIEKLSppgREIKIVQVQID----DVGKIQTKLDRLVGRLEDAERAADVLVDagfaaDTTQTREQISTLRKTLG 3008
Cdd:TIGR02168  861 IEELEELIEELE---SELEALLNERAsleeALALLRSELEELSEELRELESKRSELRR-----ELEELREKLAQLELRLE 932
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227  3009 RLDNRVRdhednlhSTLKALREFYdhqSQTLDDIQdvsdefKRMKPVGSELDQIRRQQEDFRNFRER--KVEPLAIN 3083
Cdd:TIGR02168  933 GLEVRID-------NLQERLSEEY---SLTLEEAE------ALENKIEDDEEEARRRLKRLENKIKElgPVNLAAIE 993
SPEC smart00150
Spectrin repeats;
3029-3133 1.50e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.64  E-value: 1.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3029 REFYDHQSQTLDDIQDVsDEFKRMKPVGSELDQIRRQQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSagSGVSTTAIE 3108
Cdd:smart00150    1 QQFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAF-EAELEAHEERVEALNELGEQLIEE--GHPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   3109 KDLEKLNDRWNDLKERMNERDRRLD 3133
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2669-3384 1.94e-06

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: 54.69  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2669 VKRDLDRIQ-------QQWEKLRREAvdrhtrlqtcmEHCKKYSqtsetflawlrtaedkladltpgvlskaKLETRLRD 2741
Cdd:TIGR02169  182 VEENIERLDliidekrQQLERLRRER-----------EKAERYQ----------------------------ALLKEKRE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2742 LqtfrsEVWKHSGEFENT---KGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDL---------------------IA 2797
Cdd:TIGR02169  223 Y-----EGYELLKEKEALerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnkkikdlgeeeqlrvkekIG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2798 RAH-EIENCSRRLDDFNDELRNLDHSLGRCEDRL----AAHDALGGAAKDPKLleRVKAIREELTNLSKPLQSLKALAKD 2872
Cdd:TIGR02169  298 ELEaEIASLERSIAEKERELEDAEERLAKLEAEIdkllAEIEELEREIEEERK--RRDKLTEEYAELKEELEDLRAELEE 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2873 ISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETE----IEKLSPPGR 2948
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedkALEIKKQEW 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2949 EIKIVQVQIDDVGK----IQTKLDRLVGRLEDAER-------AADVLVDA--GFAADTTQTREQISTLRKTL-------- 3007
Cdd:TIGR02169  456 KLEQLAADLSKYEQelydLKEEYDRVEKELSKLQRelaeaeaQARASEERvrGGRAVEEVLKASIQGVHGTVaqlgsvge 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3008 -----------GRLDNRVRDHEDNLHSTLKALREfydHQSQTLDDIqdvsdEFKRMKPVGSELDQIRRQQE-----DFRN 3071
Cdd:TIGR02169  536 ryataievaagNRLNNVVVEDDAVAKEAIELLKR---RKAGRATFL-----PLNKMRDERRDLSILSEDGVigfavDLVE 607
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3072 FrERKVEP--------------------LAINVDKVNVAGrDLV----------RSAGSGVSTTAIEK--------DLEK 3113
Cdd:TIGR02169  608 F-DPKYEPafkyvfgdtlvvedieaarrLMGKYRMVTLEG-ELFeksgamtggsRAPRGGILFSRSEPaelqrlreRLEG 685
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3114 LNDRWNDLKERMNERDRRLDVALL---------------------QSGKFQEALAGLSKWLSDTEEMVANQKPPSSDYKV 3172
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQelsdasrkigeiekeieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3173 VKAQLQEQKF-LKKML--LDRQNSMGSLANLGKEVANHCEpgERASIEKQLNDLMKRFDALTdgaeQRELDLEEAMEvak 3249
Cdd:TIGR02169  766 RIEELEEDLHkLEEALndLEARLSHSRIPEIQAELSKLEE--EVSRIEARLREIEQKLNRLT----LEKEYLEKEIQ--- 836
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3250 rfhDKISPLELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEILGKKPDFS-DLADVTAQLMHLVSDEEAVN--LG 3326
Cdd:TIGR02169  837 ---ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKkERDELEAQLRELERKIEELEaqIE 913
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3327 EKVRGVTERYTGLVDASDNIGALLAESRQGLR--HLVLSYQDLVAWMESMEAELKRFKSV 3384
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRALEPV 973
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4333-4437 2.92e-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: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4333 KEATEFHDTLQAFVEWLTQAEKLLSNaEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKGTHLKYfSQKQDVILI 4412
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 221330227  4413 KNLLVSVQHRWERVVSKAAERTRAL 4437
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3967-4297 3.24e-06

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: 53.92  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3967 EPDK-PEVKKHIEDLDNAWDNITALYAKREE---NLIDAMEKAMEFHETLQNLLKFLTKAEDKFAH-LGAVGSDIDAVKR 4041
Cdd:TIGR02169  672 EPAElQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4042 QIEQLKSFKDEVDPHMVEVE----ALNRQAVELTERTSPEQAASIREPLSVVN---RRWEALLRGmVERQKQLEHALLHL 4114
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEedlhKLEEALNDLEARLSHSRIPEIQAELSKLEeevSRIEARLRE-IEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4115 GQ--FQHALNELLVWINKTDSTLDQLKPIPGDPQLLEVELAKLKVLANDIQA-HQNSVDTLNDAGRQLIETEKGSVEAST 4191
Cdd:TIGR02169  831 LEkeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrLGDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4192 TQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEVQDilgwLGDVDAV-------IGASKPVGGLpetATEQLER 4264
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAElqrveeeIRALEPVNML---AIQEYEE 983
                          330       340       350
                   ....*....|....*....|....*....|...
gi 221330227  4265 FMEVYNELDENRPKVETIQAQGQEYIKRQNQMK 4297
Cdd:TIGR02169  984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
SPEC smart00150
Spectrin repeats;
2596-2695 3.24e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 3.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   2596 RHFAENCSKTLGWLGGELSNLTDRLlVSAHKPTLQHQIDTHEPIYREVMAREHEVIMLINKGKDLTDRQQDRG--VKRDL 2673
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAeeIEERL 79
                            90       100
                    ....*....|....*....|..
gi 221330227   2674 DRIQQQWEKLRREAVDRHTRLQ 2695
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4558-4656 3.47e-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: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4558 QFSDALGELLDWLKKAKSRLNENGPVHgDLETVQGLCEHHKHIEQDLQKRAAQMQGVLKTGRDLERSGN--NPEVGRQLD 4635
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHyaSEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 221330227  4636 EMQSIWEEVKSAVAKRGERLQ 4656
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
3786-3890 4.05e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 4.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3786 QFSDKLEGMLRALANTVDQVNQlDPLSALPQKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIakagNKADPAVRDIK 3865
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI----EEGHPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   3866 AKLEKLNNLWNDVQNATKKRGSSLD 3890
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4032-4108 4.61e-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: 48.47  E-value: 4.61e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227  4032 VGSDIDAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTERtSPEQAASIREPLSVVNRRWEALLRGMVERQKQLE 4108
Cdd:pfam00435   29 YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLE 104
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2733-3133 5.51e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2733 AKLETRLRDLQTFRSEVwkhSGEFENTKGLGETFLSSCDiDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDF 2812
Cdd:PRK02224  202 KDLHERLNGLESELAEL---DEEIERYEEQREQARETRD-EADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2813 NDELRNLDHSLGRCEDRLAahDALGGAAKDPKLLERVKAIREELtnlSKPLQSLKALAKDISAEARAAGGDADHLTSEVD 2892
Cdd:PRK02224  278 AEEVRDLRERLEELEEERD--DLLAEAGLDDADAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2893 GLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSL--------------GIDLNDLETEIEKLSPPGREIKivqvqiD 2958
Cdd:PRK02224  353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELeeeieelrerfgdaPVDLGNAEDFLEELREERDELR------E 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2959 DVGKIQTKLDRLVGRLEDAERAADV---------LVDAGFAADTTQTREQISTLRKTLGRLDNRVRDHE----------- 3018
Cdd:PRK02224  427 REAELEATLRTARERVEEAEALLEAgkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEerleraedlve 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3019 -----DNLHSTLKALREFYDHQSQTLDDIQDVSDEF-KRMKPVGSELDQIRRQQEDFRNFRERKVEPLA-INVDKVNVAG 3091
Cdd:PRK02224  507 aedriERLEERREDLEELIAERRETIEEKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAeLNSKLAELKE 586
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 221330227 3092 R--DLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLD 3133
Cdd:PRK02224  587 RieSLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA 630
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
5166-5367 5.57e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 53.00  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5166 SRPSRSSLSASTPDSLSdnegshGGPSGRYTPRKVT---------YTSTRTGLTPGGSRAGSKPNSrplsrqgSKPPSRh 5236
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTT------GLPSSTHVPTNLTapastgptvSTADVTSPTPAGTTSGASPVT-------PSPSPR- 495
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5237 gstlsldstDDHTPSRIPQRkpsTGSTASGTTPRPARLSVT---TTTTPgsrlNGTSTITRKTASGSASPAPTSNGgmsr 5313
Cdd:pfam05109  496 ---------DNGTESKAPDM---TSPTSAVTTPTPNATSPTpavTTPTP----NATSPTLGKTSPTSAVTTPTPNA---- 555
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  5314 SSSIPALTGFGFKPIRRNISGSSTPSGMQTPRKSSAEPTF------SSTMRRTSRGTTPT 5367
Cdd:pfam05109  556 TSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVgetspqANTTNHTLGGTSST 615
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4945-5014 7.75e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.63  E-value: 7.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4945 RLTDLFRKMDKDNNGMIPRDVFIDgiLNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALRPDWQERK 5014
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA 137
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3213-3904 8.91e-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: 8.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3213 RASIEKQLNDL------MKRFDALTDgaEQRELDLEEAMEVAKRFHDKISPLELWLDNTERSVKAME-LIPTDEEKIQQR 3285
Cdd:TIGR02168  195 LNELERQLKSLerqaekAERYKELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTaELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3286 IREHDRLHDEILGKKPDF----SDLADVTAQLMHLvsDEEAVNLGEKVRGVTERYTGLVDASDNIGALLAESRQGLrhlv 3361
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELyalaNEISRLEQQKQIL--RERLANLERQLEELEAQLEELESKLDELAEELAELEEKL---- 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3362 lsyQDLVAWMESMEAELKRFKsvpvyaEKLLEQMDHLLELNENIAGHASNVESTVESGAELMKHISNdeaiqLKDKLDSL 3441
Cdd:TIGR02168  347 ---EELKEELESLEAELEELE------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-----LEARLERL 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3442 QRRYGDLTNRGGDLLKSAQNA-LPLVQQFHEAHNRLVEWMQSAEAALAPSEPRQADVLR--------LEGELADMRPILD 3512
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEeaeqaldaAERELAQLQARLD 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3513 SINQ-------------------------VGPQLCQLSPGEG---------AATIESIVTRDN----RRFDSIVEQIQRK 3554
Cdd:TIGR02168  493 SLERlqenlegfsegvkallknqsglsgiLGVLSELISVDEGyeaaieaalGGRLQAVVVENLnaakKAIAFLKQNELGR 572
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3555 AERLHLSNQRAKEVTGDIDELLEWFREMDTTLREADLPAMEPKLVRAQLQEHRSINDDI-------SSQKGRVRDVTAAS 3627
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLdnalelaKKLRPGYRIVTLDG 652
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3628 KKVLRE---SPQSENTATL----REKLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDMEQQISRLS 3700
Cdd:TIGR02168  653 DLVRPGgviTGGSAKTNSSilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3701 MPALR--------PDQITLQQDKNERLLQSIAEhkpLLDKLNKTGEALGALVAD------------DDGAKINEILDTDN 3760
Cdd:TIGR02168  733 KDLARleaeveqlEERIAQLSKELTELEAEIEE---LEERLEEAEEELAEAEAEieeleaqieqlkEELKALREALDELR 809
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3761 ARYAALRLELRERQQALESALQESSQFSDKLEGMLRALANTVDQV-------------------------NQLDPLSALP 3815
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleelieeleseleallNERASLEEAL 889
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3816 QKIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSV 3895
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969

                   ....*....
gi 221330227  3896 AEPFWKQLN 3904
Cdd:TIGR02168  970 ARRRLKRLE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2520-3288 1.05e-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: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2520 QENLRKIENLERQLEGQ-RPLLADVEQsaatlcnilgdpASR-ADVNSRVAALEKQYLALQKK-LDTKKAETEASLRDGR 2596
Cdd:TIGR02168  185 RENLDRLEDILNELERQlKSLERQAEK------------AERyKELKAELRELELALLVLRLEeLREELEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2597 HFAENCSKTLGWLGGELSNLtdRLLVSAHKPTLQHQIDTHEPIYREVMAREHEvIMLINKGKDLTDRQQDRgVKRDLDRI 2676
Cdd:TIGR02168  253 EELEELTAELQELEEKLEEL--RLEVSELEEEIEELQKELYALANEISRLEQQ-KQILRERLANLERQLEE-LEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2677 QQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAK------------------LETR 2738
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqlelqiaslnneierLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2739 LRDLQTfRSEVWKHSGEfENTKGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRN 2818
Cdd:TIGR02168  409 LERLED-RRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2819 LDHSLGRCEDRLAAHDALGGAAKDpkllerVKAIREELTNLSKPL-QSLKALAKDISAEARAAGGDADHLTseVDGLADR 2897
Cdd:TIGR02168  487 LQARLDSLERLQENLEGFSEGVKA------LLKNQSGLSGILGVLsELISVDEGYEAAIEAALGGRLQAVV--VENLNAA 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2898 MSELQGRLDDRCG-----ELQSAATAVSQFNEQMKSLGID-----LNDLETEIEKLSPPGREIkIVQVQIDDVGKIQTKL 2967
Cdd:TIGR02168  559 KKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREILKNIEgflgvAKDLVKFDPKLRKALSYL-LGGVLVVDDLDNALEL 637
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2968 DRLVGRLEDAERAADVLVDAGFAAdTTQTREQISTL---RKTLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTLDDIQD 3044
Cdd:TIGR02168  638 AKKLRPGYRIVTLDGDLVRPGGVI-TGGSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3045 VSDEFKRMKpvgselDQIRRQQEDFRNFrERKVEPLAinvDKVNVAGRDLVRSAgsgVSTTAIEKDLEKLNDRWNDLKER 3124
Cdd:TIGR02168  717 LRKELEELS------RQISALRKDLARL-EAEVEQLE---ERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAE 783
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3125 MNERDRRLDVALLQSGKFQEALAGLSKWLSDTEEMVANQKppsSDYKVVKAQLQEQKFLKKMLLDRQNSM-GSLANLGKE 3203
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELsEDIESLAAE 860
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3204 VANHCEPGERasIEKQLNDLMKRFDALTDGAEQRELDLEEAMEVAKRFHDKISPLELWLDNTERSVKAMELiptDEEKIQ 3283
Cdd:TIGR02168  861 IEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLE 935

                   ....*
gi 221330227  3284 QRIRE 3288
Cdd:TIGR02168  936 VRIDN 940
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
34-141 1.20e-05

third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409180  Cd Length: 134  Bit Score: 48.07  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLEVL-------SGEHLPREKGKMRFHMLQNAQMALDFLR 106
Cdd:cd21331    18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 221330227  107 YK-KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQI 141
Cdd:cd21331    96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2260-3246 1.40e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2260 RLNDRQHELDNLN---EELRKQYENLKGLAQFLERIQ------RQLPKE-SVSNKDEAERCIKQARKILEDMYEK----Q 2325
Cdd:TIGR02168  180 KLERTRENLDRLEdilNELERQLKSLERQAEKAERYKelkaelRELELAlLVLRLEELREELEELQEELKEAEEEleelT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2326 SLLDTTKAQVkDILRRKSdvpgaEQLRQENDSIQEKWKNLN---DICKNRIAF-SEKLRDFLDTHGNLKSWLDSKERMLt 2401
Cdd:TIGR02168  260 AELQELEEKL-EELRLEV-----SELEEEIEELQKELYALAneiSRLEQQKQIlRERLANLERQLEELEAQLEELESKL- 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2402 vlgpissdprmvqsqvqqvQVLREEFRTQQPQLKHFQElghdvvdhlagtpDAQAVEIKLKDILGKWDDLVGKLDDRAns 2481
Cdd:TIGR02168  333 -------------------DELAEELAELEEKLEELKE-------------ELESLEAELEELEAELEELESRLEELE-- 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2482 lggaadssKEFDAAVNRLREALQNISDNLDTLptdgdhQENLRKIENLERQLEGQRPLLADVEQSAatlcnilgDPASRA 2561
Cdd:TIGR02168  379 --------EQLETLRSKVAQLELQIASLNNEI------ERLEARLERLEDRRERLQQEIEELLKKL--------EEAELK 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2562 DVNSRVAALEKQYLALQKKLDTKKAEtEASLRDGRHFAENcsktlgwlggelsnltDRLLVSAHKPTLQHQIDTHEPIYR 2641
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEA-LEELREELEEAEQ----------------ALDAAERELAQLQARLDSLERLQE 499
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2642 EVMAREHEVIMLINKGKDLTDrqqDRGVKRDLDRIQQQWEKlRREAVDRHTRLQTCMEHCKKYSQTSEtFLAWlrTAEDK 2721
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSGLSG---ILGVLSELISVDEGYEA-AIEAALGGRLQAVVVENLNAAKKAIA-FLKQ--NELGR 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2722 LADLTPGVLSKAKLEtrlrdlqtfrsevwkhsGEFENTKGLGETFLSSCDidkepikaELQDIRDRWERLNNDLIARAHE 2801
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQ-----------------GNDREILKNIEGFLGVAK--------DLVKFDPKLRKALSYLLGGVLV 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2802 IENcsrrLDDFNDELRNLDHSL------GrceDRLAAHDALGGAAKDPK--LLERvkaiREELTNLSKPLQSLKALAKDI 2873
Cdd:TIGR02168  628 VDD----LDNALELAKKLRPGYrivtldG---DLVRPGGVITGGSAKTNssILER----RREIEELEEKIEELEEKIAEL 696
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2874 SAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEKLSppgreikiv 2953
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE--------- 767
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2954 qvqiDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaADTTQTREQISTLRKTLGRLDNRVRDHEDNLHSTLKALREFYD 3033
Cdd:TIGR02168  768 ----ERLEEAEEELAEAEAEIEELE------------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3034 HQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAgRDLVRSAGSGVSTT--AIEKDL 3111
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-LALLRSELEELSEElrELESKR 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3112 EKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLskwLSDTEEMVANQKPpssdyKVVKAQLQEQKFLKKmlLDRQ 3191
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALEN-----KIEDDEEEARRRLKR--LENK 980
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 221330227  3192 nsmgsLANLGkevanhcePGERASIEkQLNDLMKRFDALTdgaEQRElDLEEAME 3246
Cdd:TIGR02168  981 -----IKELG--------PVNLAAIE-EYEELKERYDFLT---AQKE-DLTEAKE 1017
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
39-136 1.56e-05

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409172  Cd Length: 145  Bit Score: 48.12  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNK---------HLKKANRRVVDLFEDLRDGHNLLSLLEVLS----GEHLPREKGKMRFHMLQNAQMALDFL 105
Cdd:cd21323    25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQpdtiDERAINKKKLTPFTISENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIWTII 136
Cdd:cd21323   105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
SPEC smart00150
Spectrin repeats;
1891-1995 1.66e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 1.66e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   1891 QGVQDALDSLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVE 1970
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD--AEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 221330227   1971 SNLNDVTVKFEKLYEKANKRGEFLD 1995
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
33-252 2.00e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 51.09  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   33 DERDAIQKKTFTKWVNKHLkkANRRVVDLFEDLRDGHNLLSLLEVLSGE---HLPREK-------GKMRFHMLQNAQMAL 102
Cdd:COG5069   374 DAEGEFEARVFTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKkqpasgiEENRFKAFENENYAV 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  103 DFLRYKKIKLVNIRAEDIVDGNpKLTLGLIW-------TIILHFQ------ISDI----VVGKEDNVSAREALLRWARRS 165
Cdd:COG5069   452 DLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLkkdgcgLSDSdlcaWLGSLGLKGDKEEGIRSFGDP 530
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  166 TARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNdrprerLETAFHIVEKEYGVTRLLdPEDVDTNEPdEKSL 245
Cdd:COG5069   531 AGSVSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARS------LAISSKILRSLGAIIKFL-PEDINGVRP-RLDV 602

                  ....*..
gi 221330227  246 ITYISSL 252
Cdd:COG5069   603 LTFIESL 609
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
32-139 2.12e-05

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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: 409155  Cd Length: 121  Bit Score: 47.03  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKgkmrFHM--------LQNAQMALD 103
Cdd:cd21306    10 APDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHS----FHLtptsfeqkVHNVQFAFE 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 221330227  104 FLRYKKIKLVNIRAEDIVDGNPKLTLGLIWTIILHF 139
Cdd:cd21306    86 LMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2837-3250 2.19e-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: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2837 GGAAKDPKLLERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAA 2916
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2917 TAVSQFNEQMKSLGIDLNDLETEIEKLsppgreIKIVQVQIDDVGKIQTKLDRLVGRLEDAEraadvlvdagfaadTTQT 2996
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKEL------EARIEELEEDLHKLEEALNDLEARLSHSR--------------IPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2997 REQISTLRKTLGRLDNRVRDHEDNLHStLKALREFYDHQSQTLDDIQDVSDEFKRMkpvgseldqIRRQQEDFRNFRERK 3076
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKS---------IEKEIENLNGKKEEL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3077 VEPLAinvdKVNVAGRDLVRSAGSgvsttaIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDT 3156
Cdd:TIGR02169  867 EEELE----ELEAALRDLESRLGD------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3157 EEMVANQKPPSS---DYKVVKAQLQEqkflkkmLLDRQNSMGSLANLGKEvanhcepgERASIEKQLNDLMKRFDALTdg 3233
Cdd:TIGR02169  937 EDPKGEDEEIPEeelSLEDVQAELQR-------VEEEIRALEPVNMLAIQ--------EYEEVLKRLDELKEKRAKLE-- 999
                          410
                   ....*....|....*...
gi 221330227  3234 AEQREL-DLEEAMEVAKR 3250
Cdd:TIGR02169 1000 EERKAIlERIEEYEKKKR 1017
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
273-482 2.69e-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: 48.60  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  273 RVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRsDEVSARKREKSKLIQIYKELEryfETVGEVDVE 352
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALE-AELAAHEERVEALNELGEQLI---EEGHPDAEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  353 AELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRlADKVQREIKHVDQKLTDLEgrIGEEGRRIERLHpvdakSIV 432
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELL-----KKH 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 221330227  433 EALETEIRHLEEPIQDMNQDCHVL-NEGRYPHVSELHKKVNKLHQRWAQLR 482
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELL 199
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3571-3670 2.84e-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: 46.16  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3571 DIDELLEWFREMDTTLREADLPAMEPKlVRAQLQEHRSINDDISSQKGRVRDVTAASKKVLRESPQSenTATLREKLDDL 3650
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 221330227  3651 KEIVDTVAQLCSERLGILEQ 3670
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
39-136 3.00e-05

first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409174  Cd Length: 148  Bit Score: 47.36  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNK---------HLKKANRRVVDLFEDLRDGHNLLSLLEV----LSGEHLPREKGKMRFHMLQNAQMALDFL 105
Cdd:cd21325    25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLsvpdTIDERAINKKKLTPFIIQENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIWTII 136
Cdd:cd21325   105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
SPEC smart00150
Spectrin repeats;
2382-2482 3.16e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 3.16e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   2382 FLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRTQQPQLKHFQELGHDVVDhlAGTPDAQAVEIKL 2461
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   2462 KDILGKWDDLVGKLDDRANSL 2482
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2238-2944 3.18e-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: 50.83  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2238 SELSPVQQQLSEINNRYGLIGVRLNDRQHELDNLNEELRKQYENLKGLAqfLERIQRQLpkesvsnkDEAERCIKQARKI 2317
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAEL--------EELEEELEELQEE 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2318 LEDMYEKQSLLDTTKAQVKDILRrksdvpgaeQLRQENDSIQEKWKNLNDIcknriafsekLRDFLDTHGNLKSWLDSKE 2397
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALD---------AAERELAQLQARLDSLERL----------QENLEGFSEGVKALLKNQS 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2398 RMLTVLGPISSdprmvqsqvqqVQVLREEFRT----------QQPQLKHFQELGhDVVDHLAGTPDAQAVEIKLKDILGk 2467
Cdd:TIGR02168  517 GLSGILGVLSE-----------LISVDEGYEAaieaalggrlQAVVVENLNAAK-KAIAFLKQNELGRVTFLPLDSIKG- 583
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2468 wDDLVGKLDDRANSLGGAADSSKEFDAAVNRLREALQNISDNLDTLPTDGDHQENLRKIENLER--QLEGQ--RPLLADV 2543
Cdd:TIGR02168  584 -TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivTLDGDlvRPGGVIT 662
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2544 EQSAATLCNILGDPASRADVNSRVAALEKQYLALQKKLDTKKAEteaslrdgrhfaencsktlgwlggeLSNLTDRLlvs 2623
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE-------------------------LEELEEEL--- 714
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2624 ahkptlqhqidthepiyREVMAREHEVimlinkgkdltdRQQDRGVKRDLDRIQQQWEKLRREAVDRHTRLQTCMEHCKK 2703
Cdd:TIGR02168  715 -----------------EQLRKELEEL------------SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2704 YSQTSETFLAWLRTAEDKLADLtpgvlsKAKLETRLRDLQTFRSEVWKHSGEFENTKGLG---ETFLSSCDIDKEPIKAE 2780
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERR 839
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2781 LQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAH-DALGgaakdpKLLERVKAIREELTNL 2859
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrSELE------ELSEELRELESKRSEL 913
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2860 SKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRL-DDRCGELQSAATAVSQFNEQMKSLG-IDLNDLE 2937
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGpVNLAAIE 993

                   ....*..
gi 221330227  2938 tEIEKLS 2944
Cdd:TIGR02168  994 -EYEELK 999
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1558-2116 4.37e-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: 4.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1558 REKIDELRNQINALKQIKDEIESQqrpVATCLEQIRQI------------VLTGGDVLSAPEVTTLENSGRELRSRVD-- 1623
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAE---LQELEEKLEELrlevseleeeieELQKELYALANEISRLEQQKQILRERLAnl 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1624 -----RVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVRE-FVSDVIGHQAD 1697
Cdd:TIGR02168  315 erqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1698 LRfitmAAQKFVDESKEFLAILNDFRTSLPERLPHV--EPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQ 1775
Cdd:TIGR02168  395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1776 REYQDALDKANEWLRSVHPRVSRI--ISEPIAGDPKGVQDQMNEAKALHN------ELLS-------------SGRL--- 1831
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGilgvlsELISvdegyeaaieaalGGRLqav 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1832 -VDNAQQALDN---LLRSLGG--------QLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTL---------VQS 1890
Cdd:TIGR02168  551 vVENLNAAKKAiafLKQNELGrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDD 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1891 qgVQDALD----------------SLVGW---VNQAEDKFKM-------NLRPASLIKERLQEQIREHKVLLADLQS--- 1941
Cdd:TIGR02168  631 --LDNALElakklrpgyrivtldgDLVRPggvITGGSAKTNSsilerrrEIEELEEKIEELEEKIAELEKALAELRKele 708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1942 ------HQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDV---YNRLSRYLDEISTVE 2012
Cdd:TIGR02168  709 eleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEAEAEIEELE 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2013 QRMASLQEALDSRETSLLSTE----ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTdTGVLRDRIKALESQWRN 2088
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEEL 867
                          650       660
                   ....*....|....*....|....*...
gi 221330227  2089 INISIDERAKLSKQKAEQQLAYEGLKDQ 2116
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSE 895
EF-hand_7 pfam13499
EF-hand domain pair;
4943-5007 5.81e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 5.81e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227  4943 KSRLTDLFRKMDKDNNGMIPRDVFIDGI--LNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5007
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1501-2119 5.97e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1501 LEVIQREISEAESGYETAEKRiKQAVFEKFNMCEENVNDLLKWVTTVEQKISsvggprEKIDELRNQINALKQIKDEIES 1580
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELE------ELEAELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1581 QQRPVATCLEQIRQIvltggdvlsAPEVTTLENSGRELRSRVDRVNDRTVRLLRRLEAG------------RDELTKLRS 1648
Cdd:TIGR02168  384 LRSKVAQLELQIASL---------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQE 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1649 ELDVFSDWLQVARRTLEDKERSL----SDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKF------------VDES 1712
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALdaaeRELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisVDEG 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1713 KEfLAILndfrTSLPERLPHVepLSSAESPIRQEvslVSAQYKDLLNRVNALQdrVSGLGGRQREYQDALDKANewlrsv 1792
Cdd:TIGR02168  535 YE-AAIE----AALGGRLQAV--VVENLNAAKKA---IAFLKQNELGRVTFLP--LDSIKGTEIQGNDREILKN------ 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1793 HPRVSRIISEPIAGDPKgvqdqmneAKALHNELLSSGRLVDNAQQALdNLLRSLG--------------------GQLSP 1852
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPK--------LRKALSYLLGGVLVVDDLDNAL-ELAKKLRpgyrivtldgdlvrpggvitGGSAK 667
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1853 MEINQLEL--PIADLKNNYQQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIKERLQEQIR 1930
Cdd:TIGR02168  668 TNSSILERrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI--SALRKDLARLEAEVEQL 745
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1931 EHKVllADLQSHQASIDSVQVSAKHLLASASNARIAkkVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRLSRYLDEIST 2010
Cdd:TIGR02168  746 EERI--AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2011 VEQRMASLQEALDSRETSLLSTEELARRMNElsrDKDQLAPQFEDCVRSGKDLIS-------LRDVTDTGV--LRDRIKA 2081
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESeleallnERASLEEALalLRSELEE 898
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 221330227  2082 LESQWRNINISI----DERAKLSKQKAEQQLAYEGLKDQVLS 2119
Cdd:TIGR02168  899 LSEELRELESKRselrRELEELREKLAQLELRLEGLEVRIDN 940
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
39-136 6.00e-05

first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409173  Cd Length: 145  Bit Score: 46.54  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKHLKK---------ANRRVVDLFEDLRDGHNLLSLLEV----LSGEHLPREKGKMRFHMLQNAQMALDFL 105
Cdd:cd21324    25 EKYAFVNWINKALENdpdckhvipMNPNTDDLFKAVGDGIVLCKMINFsvpdTIDERTINKKKLTPFTIQENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIWTII 136
Cdd:cd21324   105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
4945-5007 7.77e-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: 7.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330227 4945 RLTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5007
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
2524-3305 7.78e-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: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2524 RKIE--NLERQLEGQRPLLADVEQSAATLcnilgdPASRADVNSRVAALEKQYLALQKKLDT--KKAETEASLRDG---- 2595
Cdd:TIGR00606  326 RELEklNKERRLLNQEKTELLVEQGRLQL------QADRHQEHIRARDSLIQSLATRLELDGfeRGPFSERQIKNFhtlv 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2596 RHFAENCSKTLGWLggeLSNLTDRLlvsahkPTLQHQIDTHE--------PIYREVMAREHEVIMLINKGKDLtdrQQDR 2667
Cdd:TIGR00606  400 IERQEDEAKTAAQL---CADLQSKE------RLKQEQADEIRdekkglgrTIELKKEILEKKQEELKFVIKEL---QQLE 467
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2668 GVKRDLDRIQQQWEKLRRE--AVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRD---- 2741
Cdd:TIGR00606  468 GSSDRILELDQELRKAERElsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkmdk 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2742 LQTFRSEVWKHS-------GEFENTKGLGETFLSscdidkepIKAELQDIRDRWERLNNDLiARAHEIENcsrrldDFND 2814
Cdd:TIGR00606  548 DEQIRKIKSRHSdeltsllGYFPNKKQLEDWLHS--------KSKEINQTRDRLAKLNKEL-ASLEQNKN------HINN 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2815 ELRNLDHSLGRCEDRLaaHDALGGAAKDPKL---LERVKAIREELTNLS----------------------------KPL 2863
Cdd:TIGR00606  613 ELESKEEQLSSYEDKL--FDVCGSQDEESDLerlKEEIEKSSKQRAMLAgatavysqfitqltdenqsccpvcqrvfQTE 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2864 QSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEK- 2942
Cdd:TIGR00606  691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEq 770
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2943 ---LSPPGREIKIVQVQIDDVGKIQtkldRLVGRLEDAERAADVLVDAGFAADTTQTREQIstlrktlgRLDNRVRDHE- 3018
Cdd:TIGR00606  771 etlLGTIMPEEESAKVCLTDVTIME----RFQMELKDVERKIAQQAAKLQGSDLDRTVQQV--------NQEKQEKQHEl 838
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3019 DNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDfrnfrerKVEPLAINVDKVNVAGRDlvrsa 3098
Cdd:TIGR00606  839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE-------QLVELSTEVQSLIREIKD----- 906
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3099 gSGVSTTAIEKDLEKLNDRWNDLKERMNERDRrldVALLQSGKFQEALAGLSKWLSDTEEMVANQKppsSDYKvvkaqlq 3178
Cdd:TIGR00606  907 -AKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVKNIHGYMKDIENKIQDGK---DDYL------- 972
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3179 eqkflkkmlLDRQNSMGSLANLGKEVANHcepgerasiEKQLNDLMKRFDALTDGAEQRELDLEEAMEVAKRfHDKISPL 3258
Cdd:TIGR00606  973 ---------KQKETELNTVNAQLEECEKH---------QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR-ENELKEV 1033
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 221330227  3259 ELWLDNTERSVKAMELIPTDEE--KIQQRIREHDRLHDEILGKKPDFSD 3305
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEhqKLEENIDLIKRNHVLALGRQKGYEK 1082
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3141-3243 8.04e-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: 8.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3141 KFQEALAGLSKWLSDTEEMVANQKPPSsDYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHcEPGERASIEKQL 3220
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 221330227  3221 NDLMKRFDALTDGAEQRELDLEE 3243
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4661-4766 8.44e-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: 8.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4661 DAEKLNARVQALFDWLDHAEHKLRyAKNAPDDEKVSREMMDIHMDFMKDLRVREREKTETFEYAEDIINKAYPDAiPIIK 4740
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 221330227  4741 NWLSIIQQRWEEVRQWAINRESKLEQ 4766
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
40-132 9.99e-05

second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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: 409146  Cd Length: 109  Bit Score: 44.86  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHLKKAN--RRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRF------HMLQNAQmALDFLRYkkik 111
Cdd:cd21297    12 EQILLRWFNYHLKAANwpRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDllqraeQVLQNAE-KLDCRKF---- 86
                          90       100
                  ....*....|....*....|.
gi 221330227  112 lvnIRAEDIVDGNPKLTLGLI 132
Cdd:cd21297    87 ---LTPTSLVAGNPKLNLAFV 104
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
157-252 1.05e-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: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  157 ALLRWARRSTaryPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHiVEKEYGVTRLLDPEDVD 236
Cdd:cd21185     5 ATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
                          90
                  ....*....|....*.
gi 221330227  237 TNEPDEKSLITYISSL 252
Cdd:cd21185    81 DPEVEHLGIMAYAAQL 96
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
39-136 1.10e-04

first calponin homology (CH) domain found in the plastin family; The plastin family includes 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. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409141  Cd Length: 145  Bit Score: 45.35  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   39 QKKTFTKWVNKHLKK---------ANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPRE---KGKMR-FHMLQNAQMALDFL 105
Cdd:cd21292    25 EKVAFVNWINKNLGDdpdckhllpMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERainKKKLTvFTIHENLTLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330227  106 RYKKIKLVNIRAEDIVDGNPKLTLGLIWTII 136
Cdd:cd21292   105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PRK01156 PRK01156
chromosome segregation protein; Provisional
3818-4367 1.13e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.74  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3818 IREQIEDNDALMDDLDKRQDAFSAVQRAANDVIakagNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAE 3897
Cdd:PRK01156  202 IKKQIADDEKSHSITLKEIERLSIEYNNAMDDY----NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3898 -----------PFWKQLNSV------MKTLKDLEETLSCQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSN 3960
Cdd:PRK01156  278 leerhmkiindPVYKNRNYIndyfkyKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3961 LmnmcgepdkpevKKHIEDLDNAWDNITALYAKREENLIDAMEKAMEFHETLQ----NLLKFLTKAEDKFAHLGAVGSDI 4036
Cdd:PRK01156  358 L------------EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDISSKV 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4037 DAVKRQIEQLKSFKDEVDPHMVEVEALNRQAVELTErTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQ 4116
Cdd:PRK01156  426 SSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTT-LGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4117 FQHAL-----NELLVWINKTDSTLDQLKPIPGDpqllEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIETEKGSVEAST 4191
Cdd:PRK01156  505 RKEYLeseeiNKSINEYNKIESARADLEDIKIK----INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI 580
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4192 TQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEvqdilgWLGDVDavigaskpvgglpetatEQLERFMEVYNE 4271
Cdd:PRK01156  581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK------SIREIE-----------------NEANNLNNKYNE 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4272 LDENRPKVETIQ----------AQGQEYIKRQNQMKVSSSNLQHTLRTLKQRWDAVVSRASDKKIKLEIALKEATEFHDT 4341
Cdd:PRK01156  638 IQENKILIEKLRgkidnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
                         570       580
                  ....*....|....*....|....*.
gi 221330227 4342 LQAFVEWLTQAEKLLSNAEPVSRVLE 4367
Cdd:PRK01156  718 INDINETLESMKKIKKAIGDLKRLRE 743
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4230-4329 1.22e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 44.23  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4230 EVQDILGWLGDVDAVIgASKPVGGLPETATEQLERFMEVYNELDENRPKVETIQAQGQEYIKRQnqmKVSSSNLQHTLRT 4309
Cdd:pfam00435    9 DADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG---HYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|
gi 221330227  4310 LKQRWDAVVSRASDKKIKLE 4329
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLE 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2669-3023 1.50e-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: 48.53  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2669 VKRDLDRIQQQWEKLR---REAVDRHTRLQTCMEHCKKYSqtsetflawlrtaedkladltpgvlskaKLETRLRDLqtf 2745
Cdd:TIGR02169  175 ALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQ----------------------------ALLKEKREY--- 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2746 rsEVWKHSGEFENT---KGLGETFLSSCDIDKEPIKAELQDIRDRWERLNNDLIARAHEIENCS--------RRLDDFND 2814
Cdd:TIGR02169  224 --EGYELLKEKEALerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEA 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2815 ELRNLDHSLGRCEDRLaaHDAlggAAKDPKLLERVKAIREELTNLSKPLQSLKAlakdisaearaaggdadhltsEVDGL 2894
Cdd:TIGR02169  302 EIASLERSIAEKEREL--EDA---EERLAKLEAEIDKLLAEIEELEREIEEERK---------------------RRDKL 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2895 ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLETEIEKLSPPGREIKIVQVQID-DVGKIQTKLDRLVGR 2973
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeELADLNAAIAGIEAK 435
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 221330227  2974 LEDAERAADVLVDAGFAADT--TQTREQISTLRKTLGRLDNRVRDHEDNLHS 3023
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
SPEC smart00150
Spectrin repeats;
524-618 1.79e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 1.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227    524 FRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKI--LNDERQQTKFSGDELALY-QQRLNQLQ 600
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVeaLNELGEQLIEEGHPDAEEiEERLEELN 83
                            90
                    ....*....|....*...
gi 221330227    601 KVYAELLSTSTKRLSDLD 618
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4946-5007 1.79e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 4946 LTDLFRKMDKDNNGMIPRDVFIDGILNTKFDTSGLEMKAVADLFDRNGEGLIDWQEFIAALR 5007
Cdd:COG5126    35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
153-252 2.05e-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: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  153 SAREALLRWARRstaRYPGVRVNDFTSSWRDGLAFSALVHRNRPDLL-DWRKARNDRPRERLETAFHIVEKEYGVTRLLD 231
Cdd:cd21312    12 TPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 88
                          90       100
                  ....*....|....*....|.
gi 221330227  232 PEDVDTNEPDEKSLITYISSL 252
Cdd:cd21312    89 PEEIVDPNVDEHSVMTYLSQF 109
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
3862-4474 2.08e-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: 48.04  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3862 RDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWKQLNSVMKTLKDLEETLScQEPPAAQPQDIKKQQvaLQEIR 3941
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQL--LKQLR 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3942 HEIDQTKPEVeqvrrhgsnlmnmcgepdkPEVKKHIEDLDNAWDniTALYAKREENLIDAMEKAMEFHETLQNLLKFLTK 4021
Cdd:TIGR00618  267 ARIEELRAQE-------------------AVLEETQERINRARK--AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4022 AEDKFAHLGAVGSDIDAVKRQIEQLKSFKDEVdphmvevealnrqavelteRTSPEQAASIREPLsvvnrrweallrgmv 4101
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-------------------RDAHEVATSIREIS--------------- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4102 ERQKQLEHALLHLGQFQHALNELLVWINKTDSTLDQLKPiPGDPQLLEVELAKLKVLAndiqAHQNSVDTLNDAGRQLIE 4181
Cdd:TIGR00618  372 CQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA-TIDTRTSAFRDLQGQLAH----AKKQQELQQRYAELCAAA 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4182 TEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQ--HELEEALREAHGYIAEVQDILGWLGDVDAVIGASKPV-GGLPETA 4258
Cdd:TIGR00618  447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdIDNPGPL 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4259 TEQLERFMEVYNELDEnrpKVETIQAQGQEYIKRQNQMKVSSSNLQHTLRTLKQRWDAvVSRASDKKIKLEIALKEATEF 4338
Cdd:TIGR00618  527 TRRMQRGEQTYAQLET---SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR-SKEDIPNLQNITVRLQDLTEK 602
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4339 HDTLQAFVEWLTQAEKLlsNAEPVSRVLETIQAQMEEHKVLQKDVST-HREAMLLLDKKGTH---LKYFSQKQDVILIKN 4414
Cdd:TIGR00618  603 LSEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLTLTQERVREhalSIRVLPKELLASRQL 680
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4415 LLVSVQHRWERVV----------SKAAERTRALDHGYKEAREFNDAWSGMMQYLQETEQVLDQIIEEATA 4474
Cdd:TIGR00618  681 ALQKMQSEKEQLTywkemlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
3738-3884 2.13e-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: 46.25  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3738 EALGALVADDDGAKiNEILDtdnaRYAALRLELRERQQALESALQESSQFSDKLEGMLRALANTVDQVN-QLDPLSALPQ 3816
Cdd:cd21116    80 ELADNLIKGDQGAK-QQLLQ----GLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQaQVAVLNALKN 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221330227 3817 KIREQIEDNDALMDDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRD-IKAKLEKLNNLWNDVQNATKK 3884
Cdd:cd21116   155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAfLQADLKAAKADWNQLYEQAKS 223
SPEC smart00150
Spectrin repeats;
3467-3558 2.15e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 2.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   3467 QQFHEAHNRLVEWMQSAEAALA----PSEPRQADVL-----RLEGELADMRPILDSINQVGPQLCQLSPGEgAATIESIV 3537
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAsedlGKDLESVEALlkkheAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 221330227   3538 TRDNRRFDSIVEQIQRKAERL 3558
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2773-3030 2.35e-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: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2773 DKEPIKAELQDIRDRWERLNndliaRAHE-IENCSRRLDDFnDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKA 2851
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLE-----RAHEaLEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2852 IREELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGL-ADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLG 2930
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2931 IDLNDLETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLVDAgFAADTTQTREQISTLRKTLGRL 3010
Cdd:COG4913   373 LPLPASAEEFAAL--------------------RAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASL 431
                         250       260
                  ....*....|....*....|
gi 221330227 3011 DNRVRDHEDNLHSTLKALRE 3030
Cdd:COG4913   432 ERRKSNIPARLLALRDALAE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3211-3956 2.51e-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: 47.76  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3211 GERASIEKQLNDLMKRFDALTDGAEQRELDLEEA--------MEVAKRFHDKISPLELWLDNTERSVKAMELIPTD-EEK 3281
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDaEER 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3282 IQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAVnLGEKVRGVTErytglVDASdnigalLAESRQGLRHLV 3361
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEE-----VDKE------FAETRDELKDYR 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3362 LSYQDLVAWMESMEAELKRFKsvpvyaEKLLEQMDHLLELNENIAGHASNVESTVESGAELMKHISNDE--AIQLKDKLD 3439
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQ------EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkLEQLAADLS 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3440 SLQRRYGDLTNRGGDLLKsaqnalplvqQFHEAHNRLVEwmqsAEAALAPSEPRQADVLRLEGEL-ADMRPILDSINQ-- 3516
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEK----------ELSKLQRELAE----AEAQARASEERVRGGRAVEEVLkASIQGVHGTVAQlg 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3517 -VGPQLCQLSPGEGAATIESIVTRDNrrfDSIVEQIQ----RKAER---LHLSNQRAKEVTGDIdellewfREMDTTLRE 3588
Cdd:TIGR02169  532 sVGERYATAIEVAAGNRLNNVVVEDD---AVAKEAIEllkrRKAGRatfLPLNKMRDERRDLSI-------LSEDGVIGF 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3589 A-DLPAMEPKLVRAQLQEHRS--INDDISSQK---GRVRDVT-----------------AASKKVLRESPQSENTATLRE 3645
Cdd:TIGR02169  602 AvDLVEFDPKYEPAFKYVFGDtlVVEDIEAARrlmGKYRMVTlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3646 KLDDLKEIVDTVAQLCSERLGILEQALPLSEHFADSHQGLTAWLDDMEQQISRLS--MPALRPDQITLQQ---DKNERLL 3720
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLEQeieNVKSELK 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3721 QSIAEHKPLLDKLNKTGEALGALVADDDGAKINEI---LDTDNARYAALRLELRERQQALESALQESSQFSDKLEGMLRA 3797
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3798 LANTVDQVN----QLDPLSALPQKIREQIEDNDALMDDLDKRqdaFSAVQRAANDVIAKaGNKADPAVRDIKAKLEKLnn 3873
Cdd:TIGR02169  842 RIDLKEQIKsiekEIENLNGKKEELEEELEELEAALRDLESR---LGDLKKERDELEAQ-LRELERKIEELEAQIEKK-- 915
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3874 lwNDVQNATKKRGSSLDDILSVAEPFWKQ----------LNSVMKTLKDLEETLSCQEP-----------PAAQPQDIKK 3932
Cdd:TIGR02169  916 --RKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPvnmlaiqeyeeVLKRLDELKE 993
                          810       820
                   ....*....|....*....|....
gi 221330227  3933 QQVALQEIRHEIDQTKPEVEQVRR 3956
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKR 1017
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
815-852 2.55e-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: 2.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 221330227  815 KQQGQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIP 852
Cdd:cd11768    11 IEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIP 48
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1642-1887 2.78e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1642 ELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKFVDESKEflailnd 1721
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1722 frtslperlphveplssAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDkANEWLRSvhpRVSRIIS 1801
Cdd:cd00176    73 -----------------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEE---KEAALAS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1802 EPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSlggqLSPMEINQLELPIADLKNNYQQLLDNLGEHCK 1881
Cdd:cd00176   132 EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQK 207

                  ....*.
gi 221330227 1882 TLDKTL 1887
Cdd:cd00176   208 KLEEAL 213
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
40-132 2.80e-04

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which 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, and are probably involved in the 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. 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: 409145  Cd Length: 109  Bit Score: 43.28  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHLKKA--NRRVVDLFEDLRDGHNLLSLLEVLSGEHL---------PREKGKMrfhMLQNAQmALDFLRYk 108
Cdd:cd21296    12 EKVLLKWMNFHLKKAgyKKTVTNFSSDVKDAEAYAYLLNVLAPEHCdpatleakdPLERAKL---VLEQAE-KMNCKRY- 86
                          90       100
                  ....*....|....*....|....
gi 221330227  109 kiklvnIRAEDIVDGNPKLTLGLI 132
Cdd:cd21296    87 ------LTAKDIVEGSANLNLAFV 104
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
34-142 2.95e-04

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409178  Cd Length: 118  Bit Score: 43.82  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLEV---------LSGEHLPREKGKMRfhMLQNAQMALDF 104
Cdd:cd21329     2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 221330227  105 LRYK-KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21329    78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2777-2943 3.38e-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: 45.69  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2777 IKAELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALggAAKDPKLLERVKAIREeL 2856
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--IKKYEEQLGNVRNNKE-Y 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2857 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAatavsqfneqmkslgidLNDL 2936
Cdd:COG1579    92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE-----------------LAEL 154

                  ....*..
gi 221330227 2937 ETEIEKL 2943
Cdd:COG1579   155 EAELEEL 161
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-497 3.63e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  306 EMKRLLSDLQRFRSDEVSARKREK------------SKLIQIYKELERYFETVGEVDVEaELRPDA--IEKAWYRMNTaL 371
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLE-ELEKKAeeYEKLKEKLIK-L 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  372 QDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEGRIGEEG--------RRIERLHP--------VDAKSIVEAL 435
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleERLKELEPfyneylelKDAEKELERE 617
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227  436 ETEIRHLEEPIQDMNQDCHVLNEgrypHVSELHKKVNKLHQRWAQLR----TNFHTNLVQKLSGLK 497
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEK----RLEELRKELEELEKKYSEEEyeelREEYLELSRELAGLR 679
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1537-1712 3.70e-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: 45.13  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1537 VNDLLKWVTTVEQKISSvGGPREKIDELRNQINALKQIKDEIESQQRPVATCLEQIRQIVLTGgdvlsAPEVTTLENSGR 1616
Cdd:cd00176     9 ADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1617 ELRSRVDRVNDRTVRLLRRLEAGRDELTKLRsELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADSVREFVSDVIGHQA 1696
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHEP 160
                         170
                  ....*....|....*.
gi 221330227 1697 DLRFITMAAQKFVDES 1712
Cdd:cd00176   161 RLKSLNELAEELLEEG 176
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1929-2111 3.91e-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: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1929 IREHKVLLADLQSHQASIDSVQVSAKHLLASASNARI--AKKVESNLNDVtvkfekLYEKANKRGEFLDDVYNRLSRYLD 2006
Cdd:COG5391   303 FSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGvfAKRLEQNQNSI------LNEGVVQAETLRSSLKELLTQLQD 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2007 EISTVEQRMASLQEALDSRETSLLSTEELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQW 2086
Cdd:COG5391   377 EIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVSQQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDK 456
                         170       180       190
                  ....*....|....*....|....*....|
gi 221330227 2087 RNI----NISIDERAKLSKQ-KAEQQLAYE 2111
Cdd:COG5391   457 EKLeeqlAIAEKDAQEINEElKNELKFFFS 486
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
5116-5284 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 221330227 5116 TPR-RSTPNAAATASSSPHAHNGGSSnLPPYMSGQGPIikvRERS---------VRSIPMSRPSRSSLSASTPDSLSDNE 5185
Cdd:PHA03307  255 CPLpRPAPITLPTRIWEASGWNGPSS-RPGPASSSSSP---RERSpspspsspgSGPAPSSPRASSSSSSSRESSSSSTS 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 5186 GSHGGPSGRYTPRKVTYTSTRTGLTPGGSRAGSKPNSRPLSRQGSKPPSRH--------------GSTLSLDSTDDHTPS 5251
Cdd:PHA03307  331 SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASagrptrrraraavaGRARRRDATGRFPAG 410
                         170       180       190
                  ....*....|....*....|....*....|...
gi 221330227 5252 RIPQRKPSTGSTASGTTPRPARLSVTTTTTPGS 5284
Cdd:PHA03307  411 RPRPSPLDAGAASGAFYARYPLLTPSGEPWPGS 443
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
808-856 4.55e-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: 4.55e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 221330227    808 VQAICAYKQQ--GQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACL 856
Cdd:smart00326    5 VRALYDYTAQdpDELSFKKGDIITVLEKSDDGWWKGRLGRGKEGLFPSNYV 55
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2921-3136 5.19e-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: 44.74  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2921 QFNEQMKSLGIDLNDLETEIEKLSPPGREIKiVQVQIDDVGKIQTKLDRLVGRLEDAERAADVLVDAGFAADTtqtreqi 3000
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3001 stlrktlgrldnRVRDHEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMK----------------PVGSELDQIRR 3064
Cdd:cd00176    76 ------------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADdleqwleekeaalaseDLGKDLESVEE 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 3065 QQEDFRNFrERKVEPLAINVDKVNVAGRDLVRSAGSGvSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVAL 3136
Cdd:cd00176   144 LLKKHKEL-EEELEAHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
61-136 7.32e-04

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 42.82  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   61 LFEDLRDGHNLLSLL----------EVLSgehLPREKGKM--RFHMLQNAQMALDFLRYKKIKLVNIRAEDIVDGNPKLT 128
Cdd:cd21294    38 LFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPlnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114

                  ....*...
gi 221330227  129 LGLIWTII 136
Cdd:cd21294   115 LGLIWQII 122
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
943-1787 8.60e-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: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   943 LRRLRREMDEVNRLFD-EFEKRARAEEESKQASRifTEECLAIKSKLedmaRELDQIILAPLPRDL-DSLEHVLEIHSDY 1020
Cdd:TIGR02168  178 ERKLERTRENLDRLEDiLNELERQLKSLERQAEK--AERYKELKAEL----RELELALLVLRLEELrEELEELQEELKEA 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1021 ERRLHLLEPELKHLQETFRTIALKTPVLKKSLDNLMELWKEL-NTQSGLHKdRLKLLEASLAGLEDNehvISELENELAR 1099
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaNEISRLEQ-QKQILRERLANLERQ---LEELEAQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1100 HQdlpstaEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLgrmgvpTKVLGDLKRLHSNVERLNTRWSAVCNQLGERM 1179
Cdd:TIGR02168  328 LE------SKLDELAEELAELEEKLEELKEELESLEAELEEL------EAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1180 RSCETAIGLMKNLQSSVQVEeswVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENVNVAGGRLIREAKIYDskclr 1259
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDR---RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR----- 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1260 fvDWLVEARPSFSPPRRDLRPADSDPGATQYYSQRLDNLN------TKN--------DRLLEQLS--QRLKTAIEVNGSD 1323
Cdd:TIGR02168  468 --EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkalLKNqsglsgilGVLSELISvdEGYEAAIEAALGG 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1324 GLQY-----------AESLQKPLKTFRVDFSAGSVPTGDGYAARQEDLYTTtysttqisSTKTTKSSTKSVYSSDGLDAA 1392
Cdd:TIGR02168  546 RLQAvvvenlnaakkAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN--------IEGFLGVAKDLVKFDPKLRKA 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1393 -----SQEVSTAGLPQSQIQFNEIRTLKRSQQLGGHSVLD---IAGIRDPRTGRVLtigeAIQLRILDVRTgemlvgdRR 1464
Cdd:TIGR02168  618 lsyllGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSIL----ERRREIEELEE-------KI 686
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1465 ITLEQAADQGLIDLQLAKQLLEpgAGRDASGRELSLLEVIQREISEAESGYETAEKRIKQavfekfnmCEENVNDLLKWV 1544
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKEL 756
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1545 TTVEQKISSVGGPREKIDElrnqinALKQIKDEIESQQRPVATCLEQIrqivltggdvlsapevTTLENSGRELRSRVDR 1624
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEE------ELAEAEAEIEELEAQIEQLKEEL----------------KALREALDELRAELTL 814
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1625 VNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVREFVSDVI-GHQADLRFITM 1703
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERaSLEEALALLRS 894
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1704 AAQKFVDESKEFLAILNDFRTSLPERlphveplssaespiRQEVSLVSAQYKDLLNRVNALQDRVSGLGgrQREYQDALD 1783
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEEL--------------REKLAQLELRLEGLEVRIDNLQERLSEEY--SLTLEEAEA 958

                   ....
gi 221330227  1784 KANE 1787
Cdd:TIGR02168  959 LENK 962
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
32-140 9.16e-04

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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: 409186  Cd Length: 129  Bit Score: 42.67  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMR----FHMLQNAQMALDFLRY 107
Cdd:cd21337    14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
                          90       100       110
                  ....*....|....*....|....*....|...
gi 221330227  108 KKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 140
Cdd:cd21337    94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
45-125 9.23e-04

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: 41.84  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   45 KWVNKHLkkANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDF-LRYKKIKLVnIRAEDIVDG 123
Cdd:cd21184     8 EWVNSKI--PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIaEEELGIPKI-ITPEDMVSP 84

                  ..
gi 221330227  124 NP 125
Cdd:cd21184    85 NV 86
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2274-2482 9.61e-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: 43.97  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2274 ELRKQYENLKGLAQFLERIQRQLPKESVSNK-DEAERCIKQARKILEDMYEKQSLLDTTKAQVKDILRrkSDVPGAEQLR 2352
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDlESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2353 QENDSIQEKWKNLNDICKNR---IAFSEKLRDFLDTHGNLKSWLDSKERMLTVLgPISSDPRMVQSQVQQVQVLREEFRT 2429
Cdd:cd00176    79 ERLEELNQRWEELRELAEERrqrLEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221330227 2430 QQPQLKHFQELGHDVVDHlAGTPDAQAVEIKLKDILGKWDDLVGKLDDRANSL 2482
Cdd:cd00176   158 HEPRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
PLEC smart00250
Plectin repeat;
1428-1456 9.67e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.77  E-value: 9.67e-04
                            10        20
                    ....*....|....*....|....*....
gi 221330227   1428 IAGIRDPRTGRVLTIGEAIQLRILDVRTG 1456
Cdd:smart00250   10 IGGIIDPETGQKLSVEEALRRGLIDPETG 38
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2475-3048 9.67e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2475 LDDRANSLGG-----AADSSKEFDAAVNRLREALQNISDNLDTLPTDGDHQENLRkiENLERQLEGQRPLLADVEQSAAT 2549
Cdd:PRK02224  182 LSDQRGSLDQlkaqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVLEEHEERREELETLEAE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2550 LcnilgdpasrADVNSRVAALEKQYLALQKKLDTKKAETEASLRDGRHFAENCsktlgwlggELSNLtDRLLVSAHKPTL 2629
Cdd:PRK02224  260 I----------EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA---------GLDDA-DAEAVEARREEL 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2630 QHQIDTHEPIYREVMAREHEVimlinkgkdltdRQQDRGVKRDLDRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSE 2709
Cdd:PRK02224  320 EDRDEELRDRLEECRVAAQAH------------NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2710 TFLAWLRTAEDKLADLTpgvLSKAKLETRLRDLQTFRSEVWKHSGEFEntkglgetflsscdidkepikAELQDIRDRWE 2789
Cdd:PRK02224  388 ELEEEIEELRERFGDAP---VDLGNAEDFLEELREERDELREREAELE---------------------ATLRTARERVE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2790 RlNNDLIA---------------RAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKD-PKLLERVKAI- 2852
Cdd:PRK02224  444 E-AEALLEagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRiERLEERREDLe 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2853 ------REELTNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQF---- 2922
Cdd:PRK02224  523 eliaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaia 602
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2923 ---------NEQMKSLGiDLNDLETeiEKLSPPGREIKIVQVQIDDvgkiqtklDRLVGRLEDAERAADVLVDAgfAADT 2993
Cdd:PRK02224  603 daedeierlREKREALA-ELNDERR--ERLAEKRERKRELEAEFDE--------ARIEEAREDKERAEEYLEQV--EEKL 669
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221330227 2994 TQTREQISTLRKTLGRLDNRVRDhednlhstLKALREFYDHQSQTLDDIQDVSDE 3048
Cdd:PRK02224  670 DELREERDDLQAEIGAVENELEE--------LEELRERREALENRVEALEALYDE 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-639 1.06e-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: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   265 LFDMESQ-RRVHEYRDLAQQFiywcREKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYF 343
Cdd:TIGR02168  195 LNELERQlKSLERQAEKAERY----KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   344 ETVGEVdVEAELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLegrigeegrrierl 423
Cdd:TIGR02168  271 ELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------------- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   424 hpvdaKSIVEALETEIRHLEEPIQDMNQDchvlnegryphVSELHKKVNKLHQRWAQLRTNfHTNLVQKLSGLKypvHET 503
Cdd:TIGR02168  336 -----AEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQ-LETLRSKVAQLE---LQI 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   504 TVTRQTRMVVESRQIDTNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEhkiidqfhtkiLNDERQQTK 583
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE-----------LERLEEALE 464
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227   584 FSGDELALYQQRLNQLQKVYAELLStstkRLSDLDSLQ-HFLGQASAELQWLNEKEQ 639
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQA----RLDSLERLQeNLEGFSEGVKALLKNQSG 517
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1496-2008 1.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1496 RELSLLEVIQREISEAESGYETAEKRIKqAVFEKFNMCEENVNDLLKWVTTVEQKIssvGGPREKIDELRNQINALKQIK 1575
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1576 DEIESQqRPVATCLEQIRQIVLTGGDVLSAPEV--TTLENSGRELRSRVDRVNDRTVRLlRRLEAGRDELTKLRSELDVF 1653
Cdd:PRK03918  283 KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKrlSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1654 SDWLQVARRTLEDKERSLSDLTRLPSQaDSVREfvsdvighqadLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHV 1733
Cdd:PRK03918  361 HELYEEAKAKKEELERLKKRLTGLTPE-KLEKE-----------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1734 EPLSSAES-------PIRQE-----VSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDKAN---------EWLRSV 1792
Cdd:PRK03918  429 EELKKAKGkcpvcgrELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKEL 508
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1793 HPRVSRIISEP-----------------IAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSLGgQLSPMEI 1855
Cdd:PRK03918  509 EEKLKKYNLEElekkaeeyeklkeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1856 NQLELPIADLKNNY-------------QQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFkmNLRPASLIK 1922
Cdd:PRK03918  588 EELEERLKELEPFYneylelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELR 665
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1923 ERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTVKFEKLYEKANK-RGEFLDDVYNRL 2001
Cdd:PRK03918  666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKyKALLKERALSKV 745

                  ....*..
gi 221330227 2002 SRYLDEI 2008
Cdd:PRK03918  746 GEIASEI 752
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
45-129 1.10e-03

second calponin homology (CH) domain found in the family of plastin; The plastin family includes plastin-1, -2, and -3. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. 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: 409144  Cd Length: 113  Bit Score: 41.88  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   45 KWVNKHLKKA--NRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFH--------MLQNAqmalDFLRYKKIklvn 114
Cdd:cd21295    19 RWVNYHLERAgcDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTSALRESdllqraelMLQNA----DKIGCRKF---- 90
                          90
                  ....*....|....*
gi 221330227  115 IRAEDIVDGNPKLTL 129
Cdd:cd21295    91 VTPKDVVTGNPKLNL 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2777-3297 1.17e-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: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2777 IKAELQDIRDRWERLNNdliarahEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAhdalggaakdpkLLERVKAIREEL 2856
Cdd:COG1196   258 LEAELAELEAELEELRL-------ELEELELELEEAQAEEYELLAELARLEQDIAR------------LEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2857 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDL 2936
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2937 ETEIEKLsppgreikivqvqiddvgkiQTKLDRLVGRLEDAERAADVLvdagfAADTTQTREQISTLRKTLGRLDNRVRD 3016
Cdd:COG1196   399 AAQLEEL--------------------EEAEEALLERLERLEEELEEL-----EEALAELEEEEEEEEEALEEAAEEEAE 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3017 HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDF--------RNFRERKVEPLAINVDKVN 3088
Cdd:COG1196   454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalLLAGLRGLAGAVAVLIGVE 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3089 VAGRDLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQEALAGLSKWLSDTEEMVANQKPPSS 3168
Cdd:COG1196   534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3169 DYKVVKAQLQEQKFLKKMLLDRQNSMGSLANLGKEVANHCEPGERASIEKQLNDLMKRFDALTDGAEQRELDLEEAMEVA 3248
Cdd:COG1196   614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 221330227 3249 KRFHDKISPLELWLDNTERSVKAMELIPTDEEKIQQRIREHDRLHDEIL 3297
Cdd:COG1196   694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4102-4384 1.24e-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: 45.44  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4102 ERQKQLEHALLHLGQFQHALNELLvwiNKTDSTLDQLKPIPGDPQLLEVELAKLKVLANDIQAHQNS-VDTLNDAGRQLi 4180
Cdd:TIGR02169  206 EREKAERYQALLKEKREYEGYELL---KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEiEQLLEELNKKI- 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4181 eTEKGSVEASTTQEKLRKLNNEWKQLLQKASDRQHELEEALREAHGYIAEVQDILGWLGDVDAVIGASKpvgGLPETATE 4260
Cdd:TIGR02169  282 -KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER---KRRDKLTE 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  4261 QLERFMEVYNELdenRPKVETIQAQGQEYIKRQNQMKVSSSNLQH-------TLRTLKQRWDAVVSRASDKKIKLEIALK 4333
Cdd:TIGR02169  358 EYAELKEELEDL---RAELEEVDKEFAETRDELKDYREKLEKLKReinelkrELDRLQEELQRLSEELADLNAAIAGIEA 434
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 221330227  4334 EATEFHDTLQAFVEWLTQAE-KLLSNAEPVSRVLETIQAQMEEHKVLQKDVS 4384
Cdd:TIGR02169  435 KINELEEEKEDKALEIKKQEwKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3604-3872 1.38e-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: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3604 QEHRSINDDISSQKGRVRDVTAASKKVLRESPQSENTATLREKLDDLKEIVDTVAQLcSERLGILEQALPLSEHFADSHQ 3683
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3684 GLTAWLDDMEQQISRLSmpalrpDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEAlgALVADDDGAKINEILDtdnARY 3763
Cdd:COG4913   696 ELEAELEELEEELDELK------GEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGD---AVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3764 AALRLELRERQQALESALQESSQfsdKLEGMLRALANT-VDQVNQLDP-LSALP--QKIREQIEDndalmDDL-DKRQDA 3838
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEE---ELERAMRAFNREwPAETADLDAdLESLPeyLALLDRLEE-----DGLpEYEERF 836
                         250       260       270
                  ....*....|....*....|....*....|....
gi 221330227 3839 FSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLN 3872
Cdd:COG4913   837 KELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1558-2393 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 221330227  1558 REKIDELRNQINALKQIKDEIESQQRPvatcLEQIRQIVLTGGDvlsaPEVTTL-ENSGRELRSRVDRVNDrTVRLLRRL 1636
Cdd:TIGR00606  261 LSKIMKLDNEIKALKSRKKQMEKDNSE----LELKMEKVFQGTD----EQLNDLyHNHQRTVREKERELVD-CQRELEKL 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1637 EAGRDELTKLRSELDVFSDWLQVARRTLEDKERSlSDLTRLPSQADS-VREFVSDVIGHQADLRFITMAAQKFVDESKEF 1715
Cdd:TIGR00606  332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-RDSLIQSLATRLeLDGFERGPFSERQIKNFHTLVIERQEDEAKTA 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1716 LAILNDFRTSLPERlphveplSSAESPIRQEVSLVSaqyKDLLNRVNALQDRVSGLGGRQREYQDALDKANEWLRSVHPR 1795
Cdd:TIGR00606  411 AQLCADLQSKERLK-------QEQADEIRDEKKGLG---RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1796 VSRIISEPIAGDPKGVQDQMNEAKALHNE---LLSSGRLVDNAQQALDNLLRSLggqlspmeiNQLELPIADLKNNYQQL 1872
Cdd:TIGR00606  481 RKAERELSKAEKNSLTETLKKEVKSLQNEkadLDRKLRKLDQEMEQLNHHTTTR---------TQMEMLTKDKMDKDEQI 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1873 LDNLGEHCKTLDKTL---VQSQGVQDALDSLVGWVNQAEDKF-KMNLRPASLikERLQEQIR-EHKVLLADLQSHQASID 1947
Cdd:TIGR00606  552 RKIKSRHSDELTSLLgyfPNKKQLEDWLHSKSKEINQTRDRLaKLNKELASL--EQNKNHINnELESKEEQLSSYEDKLF 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1948 SVQVSakhllasasnariaKKVESNLNdvtvKFEKLYEKANKRGEFLDDVYNRLSRYLDEIST-----------VEQRMA 2016
Cdd:TIGR00606  630 DVCGS--------------QDEESDLE----RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrVFQTEA 691
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2017 SLQEALDSRETSLLST----EELARRMNELSRDKDQLAPQFEdcvrsGKDLISLRDVTDTGVLRDRIKALESQWRNINIS 2092
Cdd:TIGR00606  692 ELQEFISDLQSKLRLApdklKSTESELKKKEKRRDEMLGLAP-----GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2093 IDERAK-LSKQKAEQQLAYEGLKDQVLswlastearvnglppvaidldrIKQQHDELKPICKDYRDYAPTIDKInDIGAQ 2171
Cdd:TIGR00606  767 IEEQETlLGTIMPEEESAKVCLTDVTI----------------------MERFQMELKDVERKIAQQAAKLQGS-DLDRT 823
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2172 YDALiRPESPARKRSTYSPIKRTSPLRRMSGDARSPSPTKGGILSPLSTGSsgfgsrrssqdgFQLSELSPVQQQLSEin 2251
Cdd:TIGR00606  824 VQQV-NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK------------LQIGTNLQRRQQFEE-- 888
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2252 nrygligvRLNDRQHELDNLNEELRKQYENLKGLAQFLERIQRQlpKESVSNKDEAERciKQARKILEDMYEKqslLDTT 2331
Cdd:TIGR00606  889 --------QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISSKETSN--KKAQDKVNDIKEK---VKNI 953
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227  2332 KAQVKDILRRKSDvpGAE-QLRQENDSIQEKWKNLNDICKNRIAFSEKLRDF---LDTHGNLKSWL 2393
Cdd:TIGR00606  954 HGYMKDIENKIQD--GKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMrqdIDTQKIQERWL 1017
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3685-3778 1.64e-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: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3685 LTAWLDDMEQQISRLSMPALrPDQITLQQDKNERLLQSIAEHKPLLDKLNKTGEALGALVaDDDGAKINEILDTDNARYA 3764
Cdd:pfam00435   13 LESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERLEELNERWE 90
                           90
                   ....*....|....
gi 221330227  3765 ALRLELRERQQALE 3778
Cdd:pfam00435   91 QLLELAAERKQKLE 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
916-1099 1.67e-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: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   916 EQRTAIRRALNDDA--DKLLSEGDPNDPQLRRLRRE----MDEVNRLFDEFEK-RARAEEESKQASRIFtEECLAIKSKL 988
Cdd:TIGR02169  316 ELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDlRAELEEVDKEFAETR-DELKDYREKL 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   989 EDMARELDQIIlAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALKtpvLKKSLDNLMELWKELNTQsgl 1068
Cdd:TIGR02169  395 EKLKREINELK-RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSKY--- 467
                          170       180       190
                   ....*....|....*....|....*....|.
gi 221330227  1069 hKDRLKLLEASLAGLEDNehvISELENELAR 1099
Cdd:TIGR02169  468 -EQELYDLKEEYDRVEKE---LSKLQRELAE 494
SPEC smart00150
Spectrin repeats;
1083-1183 1.71e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 1.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   1083 LEDNEHVISELEnELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPtkvlgDLKRLHSNVE 1162
Cdd:smart00150    7 ADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 221330227   1163 RLNTRWSAVCNQLGERMRSCE 1183
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1596-1995 1.73e-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: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1596 VLTGGDVLSAPEVTTLENSGRELRSRVDRvndrtvrLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLt 1675
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL- 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1676 rlpsqadsvrefvsdvighQADLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHVEPLSSAESPIRQEVSLVSAQYK 1755
Cdd:TIGR02168  732 -------------------RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1756 DLLNRVNALQDRVSGLGGRQREYQDALDKANEWLRSVHPRVSRIISEpiAGDPKGVQDQMNE-AKALHNELLSSGRLVDN 1834
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR--LEDLEEQIEELSEdIESLAAEIEELEELIEE 870
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1835 AQQALDNLLRslggqlspmEINQLELPIADLKNNYQQLLDNLGEhcktLDKTLVQSQGVQDALDSLVGWVNQAEDKFKMN 1914
Cdd:TIGR02168  871 LESELEALLN---------ERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELREKLAQLELRLEGLEVR 937
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1915 LrpaslikERLQEQIRE-HKVLLADLQSHQASIDSVQVSAKHLLASASNARiakkveSNLNDVTVKFEKLYEKANKRGEF 1993
Cdd:TIGR02168  938 I-------DNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKI------KELGPVNLAAIEEYEELKERYDF 1004

                   ..
gi 221330227  1994 LD 1995
Cdd:TIGR02168 1005 LT 1006
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-705 1.77e-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: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   366 RMNTALQDREVILQqEIER-LERLQRLADKVQR------EIKHVDqkLTDLEGRIGEEGRRIERLhpvdaKSIVEALETE 438
Cdd:TIGR02168  183 RTRENLDRLEDILN-ELERqLKSLERQAEKAERykelkaELRELE--LALLVLRLEELREELEEL-----QEELKEAEEE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   439 IRHLEEPIQDMNQDchvlnegryphVSELHKKVNKLHQRWAQLRTNFHtNLVQKLSGLKypvHETTVTRQTRMVVESRQI 518
Cdd:TIGR02168  255 LEELTAELQELEEK-----------LEELRLEVSELEEEIEELQKELY-ALANEISRLE---QQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   519 DTNPHFRDLQEHIEwCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKILNDERQQTKFSGDELALYQQ-RLN 597
Cdd:TIGR02168  320 ELEAQLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   598 QLQKVYAEllststKRLSDL-DSLQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFAT 676
Cdd:TIGR02168  399 NNEIERLE------ARLERLeDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          330       340
                   ....*....|....*....|....*....
gi 221330227   677 ILDRGEALLNQQHPASKCIEAhLTALQQQ 705
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDS-LERLQEN 500
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
923-1080 1.84e-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: 43.20  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  923 RALNDDADKLLSEGDPNDPQLRRlrrEMDEVNRLFDEFEKRARAEEESKQASRI---FTEECLAIKSKLEDMARELDQIi 999
Cdd:cd00176    57 EALNELGEQLIEEGHPDAEEIQE---RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASE- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1000 laPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTI-----ALKTPVLKKSLDNLMELWKELNTQSglhKDRLK 1074
Cdd:cd00176   133 --DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELleeghPDADEEIEEKLEELNERWEELLELA---EERQK 207

                  ....*.
gi 221330227 1075 LLEASL 1080
Cdd:cd00176   208 KLEEAL 213
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
151-254 1.93e-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: 41.13  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  151 NVSAREALLRW-----ARRSTARYpgvRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDR-PRERLETAFHIVE--K 222
Cdd:cd21218     8 YLPPEEILLRWvnyhlKKAGPTKK---RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLsEEDLEKRAEKVLQaaE 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221330227  223 EYGVTRLLDPEDVdtNEPDEKSLITYISSLYD 254
Cdd:cd21218    85 KLGCKYFLTPEDI--VSGNPRLNLAFVATLFN 114
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
2493-3098 2.09e-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: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2493 DAAVNRLREALQNISDNL-----DTLPTDGDHQENLRKI----ENLERQLEGQRPLLADVEQSAATLCNILGDPASR--A 2561
Cdd:pfam12128  314 DAAVAKDRSELEALEDQHgafldADIETAAADQEQLPSWqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiA 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2562 DVNSRV-----------AALEKQYLALQKKLdtkKAETEASLRDGRHFAENCSKTLGWLGGELSNLTdrllvsAHKPTLQ 2630
Cdd:pfam12128  394 GIKDKLakireardrqlAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT------ATPELLL 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2631 HQIDTHEPIYRevmAREHevimLINKGKDLTDRQQDRGVKRDldRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSET 2710
Cdd:pfam12128  465 QLENFDERIER---AREE----QEAANAEVERLQSELRQARK--RRDQASEALRQASRRLEERQSALDELELQLFPQAGT 535
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2711 FLAWLRTAEDKLADLTPGVLSKAKLetrLR-DLQtfrSEVWKHSGEFENTKGLGETFLSSCDIDK-----EPIKAE---- 2780
Cdd:pfam12128  536 LLHFLRKEAPDWEQSIGKVISPELL---HRtDLD---PEVWDGSVGGELNLYGVKLDLKRIDVPEwaaseEELRERldka 609
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2781 ---LQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGR-----------CEDRLAAHDALGGaakdpkll 2846
Cdd:pfam12128  610 eeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdekqsekdkKNKALAERKDSAN-------- 681
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2847 ERVKAIREELTNLSKPLQSLKALAKDISAEARAAGGDAdhlTSEVDGlaDRMSELqGRLDDRCGELQSAATA-VSQFNEQ 2925
Cdd:pfam12128  682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY---WQVVEG--ALDAQL-ALLKAAIAARRSGAKAeLKALETW 755
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2926 MKSlgiDLNDLETEIEKLSPPGREIKIVQVQIDDVGKIQTKldrlVGRLEDAERAADVLVDAGFAADTTQTREQISTLRK 3005
Cdd:pfam12128  756 YKR---DLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3006 TLGRLDNRVRDHEDNLHSTLKALREFYDHQSQTL---DDIQDVSDEFKRMKPVGS---ELDQIRRQQEDFRNFRERKVEP 3079
Cdd:pfam12128  829 QLARLIADTKLRRAKLEMERKASEKQQVRLSENLrglRCEMSKLATLKEDANSEQaqgSIGERLAQLEDLKLKRDYLSES 908
                          650
                   ....*....|....*....
gi 221330227  3080 LAINVDKVNVAGRDLVRSA 3098
Cdd:pfam12128  909 VKKYVEHFKNVIADHSGSG 927
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3250-3344 2.11e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  3250 RFHDKISPLELWLDNTERSVKAMELiPTDEEKIQQRIREHDRLHDEILGKKPDFSDLADVTAQLMHLVSDEEAvNLGEKV 3329
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERL 82
                           90
                   ....*....|....*
gi 221330227  3330 RGVTERYTGLVDASD 3344
Cdd:pfam00435   83 EELNERWEQLLELAA 97
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3977-4503 2.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3977 IEDLDNAWDNITALyaKRE-ENLIDAMEKAMEFHETLQNLLKFLTKA-EDKFAHLGAVGSDIDAVKRQIEQLKSFKDEVD 4054
Cdd:PRK03918  157 LDDYENAYKNLGEV--IKEiKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4055 PHMVEVEALNRQ--AVELTERTSPEQAASIREPLSVVNRRWEAL--LRGMVERQKQLEHALLHLGQFQHALNELLVWINK 4130
Cdd:PRK03918  235 ELKEEIEELEKEleSLEGSKRKLEEKIRELEERIEELKKEIEELeeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4131 TDSTLD--------QLKPIPGDPQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIETEKgsVEASTTQEKLRKLNNE 4202
Cdd:PRK03918  315 RLSRLEeeingieeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER--LKKRLTGLTPEKLEKE 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4203 wkqlLQKASDRQHELEEALREAHGYIAEVQDILGWLGD-VDAVIGASK--PVGGLPETATEQLERFMEVYNELDENRPKV 4279
Cdd:PRK03918  393 ----LEELEKAKEEIEEEISKITARIGELKKEIKELKKaIEELKKAKGkcPVCGRELTEEHRKELLEEYTAELKRIEKEL 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4280 ETIQAQGQEYIKRQNQMKVSSSNlQHTLRTLKQRWDAVVS-RASDKKIKLEIALKEATEFhdtlqafvewltqaEKLLSN 4358
Cdd:PRK03918  469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEY--------------EKLKEK 533
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4359 AEPVSRVLETIQAQMEEHKVLQKDVSTHREAMLLLDKKgthlkyfsqkqdvilIKNLLVSVQHRWERVVSKAAERTRALD 4438
Cdd:PRK03918  534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE---------------LAELLKELEELGFESVEELEERLKELE 598
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221330227 4439 HGYKEAREFNDAwsgmMQYLQETEQVLDqiIEEATASKEPQKIKKYIGKLKETHRQLGAKQSVYD 4503
Cdd:PRK03918  599 PFYNEYLELKDA----EKELEREEKELK--KLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
32-143 2.25e-03

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin 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: 409187  Cd Length: 130  Bit Score: 41.50  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   32 ADERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLP-------REKGKMRFHmlqNAQMALDF 104
Cdd:cd21338    15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhnfyltPESFDQKVH---NVSFAFEL 91
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 221330227  105 LRYKKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISD 143
Cdd:cd21338    92 MQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2777-2921 2.42e-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: 42.99  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2777 IKAELQDIRDRWERLNNdliarahEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLErvkAIREEL 2856
Cdd:COG1579    29 LPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE---ALQKEI 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221330227 2857 TNLSKPLQSLKALAKDISAEARAAGGDADHLTSEVDGLADRMSELQGRLDDRCGELQSAATAVSQ 2921
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
34-142 2.56e-03

third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409179  Cd Length: 125  Bit Score: 41.13  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   34 ERDAIQKKTFTKWVNKhlKKANRRVVDLFEDLRDGHNLLSLLEVL---------SGEHLPREKGKMRfhMLQNAQMALDF 104
Cdd:cd21330     9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 221330227  105 LRYK-KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQIS 142
Cdd:cd21330    85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
40-87 2.70e-03

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 40.33  E-value: 2.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 221330227   40 KKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREK 87
Cdd:cd21221     3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPE 50
PRK01156 PRK01156
chromosome segregation protein; Provisional
2665-3133 4.39e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2665 QDRGVKRDLDRIQQQWEKLRREAVDRHTRLQTCMEHCKKYSQTSETFLAWLRTAEDKLADLTPGVLSKAKLETRLRDL-- 2742
Cdd:PRK01156  208 DDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIin 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2743 ------QTFRSEVWKHSGEFENTKGLGETFLSSCDIDKEPIK--AELQDIRDRWERLNNDLIARAHEIENCSRRLDDFND 2814
Cdd:PRK01156  288 dpvyknRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2815 ELRNLDHSLGRCED------RLAAH--DALGGAAKDPkllERVKAIREE-----------LTNLSKPLQSLKALAKDISA 2875
Cdd:PRK01156  368 YLKSIESLKKKIEEysknieRMSAFisEILKIQEIDP---DAIKKELNEinvklqdisskVSSLNQRIRALRENLDELSR 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2876 EARAAGGD------ADHLTSE-VDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSL-----GIDLNDLETEIEKL 2943
Cdd:PRK01156  445 NMEMLNGQsvcpvcGTTLGEEkSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeyleSEEINKSINEYNKI 524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2944 SPPGREIKIVQVQIDDVGKIQTKLDRLVGR-----LEDAERAADVLVDAGFAADTTQtreqISTLRKTLGRLDNRVRDHE 3018
Cdd:PRK01156  525 ESARADLEDIKIKINELKDKHDKYEEIKNRykslkLEDLDSKRTSWLNALAVISLID----IETNRSRSNEIKKQLNDLE 600
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3019 DNLHSTLKalrEFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFR----NFRERKVEPLAINVDKVNVAGR-- 3092
Cdd:PRK01156  601 SRLQEIEI---GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRgkidNYKKQIAEIDSIIPDLKEITSRin 677
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 221330227 3093 ----DLVRSAG----SGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLD 3133
Cdd:PRK01156  678 diedNLKKSRKalddAKANRARLESTIEILRTRINELSDRINDINETLE 726
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1501-1699 4.50e-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: 43.21  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1501 LEVIQREISEAESGYETAEKRIKQAVfEKFNMCEENVNDLLKWVTTVEQKISSVggpREKIDELRNQINALKQikdEIES 1580
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALL-KQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRA---ELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 1581 QQRPVAtclEQIRQIVLTGGD-----VLSAPEVTTLENSGRELRSRVDRVNDRTVRL---LRRLEAGRDELTKLRSELDV 1652
Cdd:COG4942   102 QKEELA---ELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELEA 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 221330227 1653 FSDWLQVARRTLE-DKERSLSDLTRLPSQADSVREFVSDVIGHQADLR 1699
Cdd:COG4942   179 LLAELEEERAALEaLKAERQKLLARLEKELAELAAELAELQQEAEELE 226
SPEC smart00150
Spectrin repeats;
727-793 5.00e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 5.00e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330227    727 HQFFGEIKDAEQWLAKRDEILNSKFSQSDfgLDQGETLLRGMQDLREELNAFGETVATLQRRAQTVV 793
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKD--LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1501-1787 5.16e-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: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1501 LEVIQREISEAESGYETAEKRIkQAVFEKFNMCEENVNDLlkwvttvEQKISsvggpREKIDELRNQINALKQIKDEIES 1580
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDL-------EARLS-----HSRIPEIQAELSKLEEEVSRIEA 812
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1581 QQRPVATCLEQirqivltggdvlSAPEVTTLENSGRELRSRVDRVNDRTVRLLRRLEAGRDELTKLRSELDVfsdwLQVA 1660
Cdd:TIGR02169  813 RLREIEQKLNR------------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE----LEAA 876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1661 RRTLEDKersLSDLTRlpsqadsvrefvsDVIGHQADLRFITMAAQKF---VDESKEFLAILNDFRTSLPERLPHVEPLS 1737
Cdd:TIGR02169  877 LRDLESR---LGDLKK-------------ERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPK 940
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 221330227  1738 SAESPIRQEVslvsAQYKDLLNRVNALQDRVSGLG----GRQREYQDALDKANE 1787
Cdd:TIGR02169  941 GEDEEIPEEE----LSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDE 990
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2779-3179 5.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2779 AELQDIRDRWERLNNDLIARAHEIENCSRRLDDFNDELRNLDHSLGRCEDRLAAHDALGGAAKDPKLLERVKAIREELTN 2858
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2859 LSKPLQSLKALAKDISAEARAAGGDADHLT-SEVDGLADRMSELQGRLDDRCGELQSAATAVSQFNEQMKSLGIDLNDLE 2937
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2938 TEiEKLsppgREIKIVQVQIDDVGKIQTKLDRLVGRLEDAERAADVLVDAGFAADTTQTREQISTLRKT--LGRLDNRVR 3015
Cdd:COG4717   241 LE-ERL----KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAeeLQALPALEE 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3016 DHEDNLHSTLKALR----EFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIRRQQEDFRNFRERKVEPLAINVDKVNVAG 3091
Cdd:COG4717   316 LEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3092 R------------DLVRSAGSGVSTTAIEKDLEKLNDRWNDLKERMNERDRRLDVALLQSGKFQealAGLSKWLSDTEEM 3159
Cdd:COG4717   396 EyqelkeeleeleEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE---AELEQLEEDGELA 472
                         410       420
                  ....*....|....*....|
gi 221330227 3160 VANQKppssdYKVVKAQLQE 3179
Cdd:COG4717   473 ELLQE-----LEELKAELRE 487
SPEC smart00150
Spectrin repeats;
4445-4550 5.73e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 5.73e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   4445 REFNDAWSGMMQYLQETEQVLdqiiEEATASKEPQKIKKYIGKLKETHRQLGAKQSVYDGTMRTGKNLLERAPkGDRPVL 4524
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL----ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 221330227   4525 DKMLIELKEQWTRVWSKSIDRQRKLE 4550
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
40-129 5.90e-03

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 40.03  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227   40 KKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKgkmrFH--------MLQNAQMALDFLRYKKIK 111
Cdd:cd21307    18 KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSE----FFltpsstseMLHNVTLALELLKEGGLL 93
                          90
                  ....*....|....*...
gi 221330227  112 LVNIRAEDIVDGNPKLTL 129
Cdd:cd21307    94 NFPVNPEDIVNGDSKATI 111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2731-3063 6.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2731 SKAKLETRLRDLQTFRSEVWKHSGEFENT-------KGLGETFLSSCDIdKEPIKAELQDIR---DRWERLNNDLIARAH 2800
Cdd:PRK03918  253 SKRKLEEKIRELEERIEELKKEIEELEEKvkelkelKEKAEEYIKLSEF-YEEYLDELREIEkrlSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2801 EIENCSRRLDDFNDELRNLDHSLGRCEdrlaahdalggaaKDPKLLERVKAIREELTNLSKPLQSLKAlaKDISAEARAA 2880
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELE-------------ERHELYEEAKAKKEELERLKKRLTGLTP--EKLEKELEEL 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2881 GGDADHLTSEVDGLADRMSELQGRLDDR---CGELQSAATAVSQFN---------EQMKSLGIDLNDLETEIEKLSPPGR 2948
Cdd:PRK03918  397 EKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGrelteehrkELLEEYTAELKRIEKELKEIEEKER 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 2949 EIKIVQVQIDDVGKIQTKLDRL---------------VGRLEDAERAA----------------------DVLVDAGFAA 2991
Cdd:PRK03918  477 KLRKELRELEKVLKKESELIKLkelaeqlkeleeklkKYNLEELEKKAeeyeklkekliklkgeikslkkELEKLEELKK 556
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330227 2992 DTTQTREQISTLRKTLGRLDNRVRD----HEDNLHSTLKALREFYDHQSQTLDDIQDVSDEFKRMKPVGSELDQIR 3063
Cdd:PRK03918  557 KLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1894-1996 7.10e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.22  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1894 QDALDsLVGWVNQAEDKFKMNLRPASLikERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNAriAKKVESNL 1973
Cdd:pfam00435    8 RDADD-LESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA--SEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 221330227  1974 NDVTVKFEKLYEKANKRGEFLDD 1996
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3897-4340 7.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3897 EPFWKQLNSVMKTLKDLEETLSCQEPPAAQPQD-IKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLmnmcgEPDKPEVKK 3975
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEElIKEKEKELEEVLREINEISSELPELREELEKL-----EKEVKELEE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3976 HIEDLDNAWDNItalyAKREENLIDAMEKAMEFHETLQNLLKFLTKAEDKFAHLgavgSDIDAVKRQIEQLKSFKDEVdp 4055
Cdd:PRK03918  236 LKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEY-- 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4056 hmveVEALNRqaVELTERTSPEQAASIREPLSVVNRRwEALLRGMVERQKQLEHALLHLGQFQHALNELLVWINKTDSTL 4135
Cdd:PRK03918  306 ----LDELRE--IEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4136 DQLKPIPGDP---QLLEVELAKLKV-------------LANDIQAHQNSVDTLNDA-------GRQLIETEKGSVEASTT 4192
Cdd:PRK03918  379 KRLTGLTPEKlekELEELEKAKEEIeeeiskitarigeLKKEIKELKKAIEELKKAkgkcpvcGRELTEEHRKELLEEYT 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4193 QEkLRKLNNEwkqlLQKASDRQHELEEALREAHGYIAEVQDILGWLGDVDAVIGASKPVGGLpetATEQLERFMEVYNEL 4272
Cdd:PRK03918  459 AE-LKRIEKE----LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY---NLEELEKKAEEYEKL 530
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330227 4273 DENRPKVETIQAQGQEYIKRQNQMKVSSSNLQHTLRTLKQRWDAVVSRASDKKIK----LEIALKEATEFHD 4340
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKELEPFYN 602
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1924-2117 9.71e-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: 9.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  1924 RLQEQIREHK--VLLADLQSHQASIDSVQVSAKhllasaSNARIAKKVESNLNDVTVKFEKLYEKANKRGEFLDDVYNRL 2001
Cdd:TIGR02168  217 ELKAELRELElaLLVLRLEELREELEELQEELK------EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227  2002 SRYLDEISTVEQRMASLQEALDSRETSLLSTE-----------ELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDvt 2070
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEaqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELE-- 368
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 221330227  2071 dtgVLRDRIKALESQWRNINisiDERAKLSKQKAEQQLAYEGLKDQV 2117
Cdd:TIGR02168  369 ---ELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARL 409
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3756-4182 9.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3756 LDTDNARYAALRLEL---RERQQALESALQESSQFSDKLEGMLRALANTVDQV---NQLDPLSALPQKIREQIEDNDALM 3829
Cdd:COG4717    83 AEEKEEEYAELQEELeelEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELEERLEELRELE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3830 DDLDKRQDAFSAVQRAANDVIAKAGNKADPAVRDIKAKLEKLNNLWNDVQNATKKRGSSLDDILSVAEPFWKQLNSVM-- 3907
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAle 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3908 KTLKDLEETL-------------SCQEPPAAQPQDIKKQQVALQEIRHEIDQTKPEVEQVRRHGSNLMNMCGEPDKPEVK 3974
Cdd:COG4717   243 ERLKEARLLLliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 3975 KHIEDL----DNAWDNITALYaKREENLIDAMEKAMEFHETLQnLLKFLTKAEDKFAHLGAvgSDIDAVKRQIEQLKSFK 4050
Cdd:COG4717   323 ELLAALglppDLSPEELLELL-DRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQ 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330227 4051 DEVDphmvEVEALNRQaveLTERTSPEQAASIREPLSVVNRRWEALLRGMVERQKQLEHALLHLGQFQHALNELlvwinK 4130
Cdd:COG4717   399 ELKE----ELEELEEQ---LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL-----E 466
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221330227 4131 TDSTLDQLKpipgdpQLLEVELAKLKVLANDIQAHQNSVDTLNDAGRQLIET 4182
Cdd:COG4717   467 EDGELAELL------QELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
 
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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