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Conserved domains on  [gi|2020023496|ref|NP_001380991|]
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microtubule-actin cross-linking factor 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
187-293 1.84e-71

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: 235.71  E-value: 1.84e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  187 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 266
Cdd:cd21240      1 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  267 DAEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
40-176 6.12e-69

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: 228.44  E-value: 6.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   40 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddv 119
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL-------------------------------- 48
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 176
Cdd:cd21188     49 PRERGRMRFHRLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7221-7296 7.06e-37

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


:

Pssm-ID: 128539  Cd Length: 73  Bit Score: 135.65  E-value: 7.06e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496  7221 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7296
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6326-6542 2.41e-31

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.87  E-value: 2.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6326 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 6405
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6406 RLEAMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 6485
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6486 KEETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHVVSSKMEERKSKLEEAL 6542
Cdd:cd00176    158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
953-1030 1.24e-30

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


:

Pssm-ID: 465730  Cd Length: 78  Bit Score: 117.70  E-value: 1.24e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  953 ISWNYLRKDLDLVQTWNLEKLRSSAPGECHQIMKNLQAHYEDFLQDSRDSVLFSVADRLRLEEEVEACKARFQHLMKS 1030
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6766-6978 1.84e-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: 122.55  E-value: 1.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6766 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6846 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 6925
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 6926 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 6978
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6547-6761 1.85e-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: 119.47  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6547 EFQNSLQEFINWLTLAEQSLNIASPPSlILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 6626
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6627 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 6706
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 6707 PVYDTTIRTGRALKEKtLLPEDSQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 6761
Cdd:cd00176    160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6106-6323 1.25e-25

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 108.69  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6106 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 6185
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6186 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQAMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 6265
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 6266 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 6323
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5343-5556 3.78e-23

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 101.37  E-value: 3.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5343 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 5422
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5423 ESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 5502
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5503 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLDQAL 5556
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
852-918 3.50e-22

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 93.10  E-value: 3.50e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  852 QLKPRSpdhvLKNT--ISVKAVCDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCFLIP 918
Cdd:pfam17902    1 PLKQRR----SPVTrpIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5888-6104 6.96e-21

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 94.82  E-value: 6.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5888 QFWETYEELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQ 5967
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5968 KAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEpMLETLENLSSRLrMPPLIPAEVDKIRECISDNKSATVELEKLQP 6047
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6048 SFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 6104
Cdd:cd00176    161 RLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4688-4902 1.11e-17

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 85.58  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4688 YQELLQDLSEKVRAVGQRLSVQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 4767
Cdd:cd00176      9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4768 ETVALPLQGLEDLAADRINRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHS 4847
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 4848 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 4902
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3878-4106 1.52e-15

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 79.41  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3878 ELQKFLQDHKEFESWLERSEKELENMHkGGSSPETLPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDmensfkEGKEP 3957
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3958 SEIgnlVKDKLKDATERYTALHSKCTRLGSHLNMLLgQYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLA 4037
Cdd:cd00176     74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLK 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 4038 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAI 4106
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
677-866 2.50e-14

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  677 LHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYS 756
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  757 AAVQSQLQWMKQLCLCVEQHVKENTAYFQFFSDARELESFLRNLQDSIKrkySCDHNTSLSRLEDLLQDSMDEKEQLIQS 836
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2020023496  837 KSSVASLVGRSKTIVQLKPRSPDHVLKNTI 866
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5778-5990 6.66e-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: 74.40  E-value: 6.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5778 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 5857
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5858 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEH 5937
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5938 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYQKAENMYAQIKEEVRQRALALDEA 5990
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4463-4682 1.29e-13

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4463 EEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTyPNSQEAENW 4542
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIE-EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4543 KKIQEELNSRWERATEVTVARQRQLEESASHLACFQAAEsQLRPWLMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 4622
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4623 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAI 4682
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1765-1800 3.81e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.58  E-value: 3.81e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2020023496 1765 LLEAQLFAGGIVDPRTGHRLTVEEAVRHNLIDQDMA 1800
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETA 36
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4877-5807 6.62e-13

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: 76.63  E-value: 6.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4877 LVELKNHWEELskktaDRQSRlkdcmqKAQKYQwhvedlvpwiedckakmsELRVTLDPVQLESSLLRSKAmlnEVEKRR 4956
Cdd:TIGR02168  195 LNELERQLKSL-----ERQAE------KAERYK------------------ELKAELRELELALLVLRLEE---LREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4957 SLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAK 5030
Cdd:TIGR02168  243 ELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5031 HQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVAQQEFLEvkqRVNSG 5110
Cdd:TIGR02168  323 AQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5111 CVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAIGRDtdsLQSQIEDVRLFLNKIHVLKLDIEASEAECRHMLEEE 5190
Cdd:TIGR02168  388 VAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5191 GTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLndattaAEEAEALQWVVGTEVEIINqqlad 5270
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELIS----- 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5271 fkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW----------NTLNKKVAQRIAQLQEALL 5339
Cdd:TIGR02168  531 --------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLG 602
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5340 HCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiqeqkllqrlLDDRKATVDML------QAEG 5403
Cdd:TIGR02168  603 VAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT------------LDGDLVRPGGVitggsaKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5404 GRIAQSAELADREKitgQLESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSE-PVGTQTA 5482
Cdd:TIGR02168  671 SILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaEVEQLEE 747
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5483 KIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDSLQARYSEIQDRCcrkaALLDQALSNARlf 5562
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELR-- 809
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5563 gedevevlnwlAEVEDKLSSVFVKDFKQDVLHRQHADHLALNEEIVNRKKNV-DQAIKNGQALLKQTTGEEVLliQEKLD 5641
Cdd:TIGR02168  810 -----------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsEDIESLAAEIEELEELIEEL--ESELE 876
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5642 GIktryaditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAtsggqsptgeqipQFQQRQKELKKEVMEHRL 5721
Cdd:TIGR02168  877 AL-----------LNERASLEEALALL---RSELEELSEELRELESKRS-------------ELRRELEELREKLAQLEL 929
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5722 VLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYeqaadaelawVAETKRKLMAL 5801
Cdd:TIGR02168  930 RLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKEL 984

                   ....*.
gi 2020023496 5802 GPIRLE 5807
Cdd:TIGR02168  985 GPVNLA 990
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4323-4570 4.01e-12

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.40  E-value: 4.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4323 QLDEFRKLVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTLVEEINCKGTSLenlimeitapdsqg 4402
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4403 ktgsilpsvgssvgsVNGYHTCKDltEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHkEANSVLQWLESKEEV 4482
Cdd:cd00176     67 ---------------IEEGHPDAE--EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4483 LKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIqEELNSRWERATEVTVA 4562
Cdd:cd00176    129 LASEDLGKDL---ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL-EELNERWEELLELAEE 204

                   ....*...
gi 2020023496 4563 RQRQLEES 4570
Cdd:cd00176    205 RQKKLEEA 212
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3581-4345 6.33e-12

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: 73.17  E-value: 6.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3581 LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRttqqdlsaLQKNQSDLKDLQDD 3660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3661 IQNRATSFATVVKDIEGFMEENQTKLSPR-----ELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSK 3735
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3736 AAKELAENKKKIDALldwvtsvgssggqlltnlpgMEQLsgaslekgaldttdgymgvnqapEKLDKQCEMMKARHQELL 3815
Cdd:TIGR02168  384 LRSKVAQLELQIASL--------------------NNEI-----------------------ERLEARLERLEDRRERLQ 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3816 SQQQnfilatqsaqafldQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLER 3895
Cdd:TIGR02168  421 QEIE--------------ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3896 SEKELenmhkggsspETLPSLLKRQGSFSEDVIshkgdlrfvtisgqkvldmeNSFKEGKEPSEIGNLVKDKLKdATERY 3975
Cdd:TIGR02168  487 LQARL----------DSLERLQENLEGFSEGVK--------------------ALLKNQSGLSGILGVLSELIS-VDEGY 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3976 TAlhSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEANVEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEK 4055
Cdd:TIGR02168  536 EA--AIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4056 LQK----------VARDI---MEIEGEPAPDHRHVQETTDSILSHF-------------QSLSYSLAERSSLLQKAIAQS 4109
Cdd:TIGR02168  614 LRKalsyllggvlVVDDLdnaLELAKKLRPGYRIVTLDGDLVRPGGvitggsaktnssiLERRREIEELEEKIEELEEKI 693
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4110 QSVQESLESLLQSIGEVEQNLEGKQV--------SSLSSGVIQEALATNMKLKQDIARQK---SSLEATREMVTRFMETA 4178
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLEEA 773
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4179 DSTTAAVLQgKLAEVSQRFEQLCLQQQEKESSLKKLlpQAEMFEH------LSGKLQQFMENKSRMLASGNQPDQDITHF 4252
Cdd:TIGR02168  774 EEELAEAEA-EIEELEAQIEQLKEELKALREALDEL--RAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4253 FQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVR 4332
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
                          810
                   ....*....|...
gi 2020023496 4333 TFQKWLKETEGSI 4345
Cdd:TIGR02168  926 QLELRLEGLEVRI 938
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7146-7216 9.43e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 9.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 7146 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 7216
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2497-2535 4.01e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 4.01e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2497 LLTKQVVDGGIIHHISGMRLSVDNAFRHGLIGEDLAEKL 2535
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1574-1612 1.05e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 51.17  E-value: 1.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1574 LLESQVIMSGLIAPETGENLSLEEGIARNLINPQMYQQL 1612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2683-2721 1.62e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 50.79  E-value: 1.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2683 VLEAQANTGGIIDTATGKRLTLASALEEKLVDENMVRII 2721
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
6988-7112 1.72e-06

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6988 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 7066
Cdd:smart00150    7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 2020023496  7067 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 7112
Cdd:smart00150   78 ----------------------RLEELNERWEELKELAEERRQKLE 101
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3408-3750 4.07e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3408 ERELKDLTtlvsQELECVNQIIISQPQEvpaqlLKALEKDAKNLQKSLSSVSDTWNsRLLHFQNAVEIEKTKVLNQHTQL 3487
Cdd:TIGR02168  676 RREIEELE----EKIEELEEKIAELEKA-----LAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3488 EGRLQDLRAWVGNKNLILNSKGSNSEIDVDSLNLCLQQYEDLKQPMAERKAQLDALAfdiqffisehaQDLSPQQNRqmL 3567
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----------EALDELRAE--L 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3568 RLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTchQQLEDLCSWVGQAERALAGHQGRTTQQDLsAL 3647
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEE-AL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3648 QKNQSDLKDLQDDIQNratsfatvvkdiegfMEENQTKLSpRELTALREKLHQAKEQYEALQEE--------TRVAQKEL 3719
Cdd:TIGR02168  890 ALLRSELEELSEELRE---------------LESKRSELR-RELEELREKLAQLELRLEGLEVRidnlqerlSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2020023496 3720 EEAVTSALQQETEKSKAAKELAENKKKIDAL 3750
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1803-1841 7.62e-06

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.17  E-value: 7.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1803 ILIRQLQTGGIIDTVTGQRLTIDEAVSNDLVAAKIALVI 1841
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
581-675 1.37e-05

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.32  E-value: 1.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   581 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYA---ETLGKLE 657
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEeieERLEELN 83
                            90
                    ....*....|....*...
gi 2020023496   658 TQYCKLKETSSFRMRHLQ 675
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2287-2325 3.74e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 44.24  E-value: 3.74e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2287 VLSAQLLDGGIFHEQTGQKLLLNEAISRGIVPSHTAVKL 2325
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1651-1689 5.27e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 5.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1651 ILEAHLATGGFSLSPSENCINLEEAFHQGLISAWLHSVL 1689
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2401-2432 3.91e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 41.16  E-value: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2401 ILERQVVTGGIIDLKRGKKVSVTLASTLGLVD 2432
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLID 32
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2363-2401 9.55e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.00  E-value: 9.55e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2363 VLMADKAISGVLDPRTQTLCSVKDAVTVGLLDKETATRI 2401
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2576-2607 1.44e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 39.62  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2576 EVQAFTGNFVDLISGQRLTLAEAKKEGLLTNE 2607
Cdd:pfam00681    3 EAQAATGGIIDPVTGERLSVEEAVKRGLIDPE 34
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
7379-7553 1.55e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7379 PSSPATPASGTKTSLQFSRC-YDKPWLVNSKAGTP-------IRDSHSPDLQLPTPEViPSSGSKLKRPTPTFHSSRTSL 7450
Cdd:PHA03307    84 SRSTPTWSLSTLAPASPAREgSPTPPGPSSPDPPPptpppasPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPAAV 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7451 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLL-ETQSACSD 7513
Cdd:PHA03307   163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGaSSSDSSSS 242
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2020023496 7514 TSESSAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 7553
Cdd:PHA03307   243 ESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1850-1879 5.09e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 5.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2020023496 1850 GLLWPESGEILPITDALEQGIVSTELAHKI 1879
Cdd:pfam00681   10 GIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1159-1338 5.42e-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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 42.05  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1159 RSIQDAELLVKGYEIKLSQEEVVlADLSALEAHWSTLRHWLSDVKDKNSVFSVLDEEiakakvvAEQMSRLTPERNLDLE 1238
Cdd:cd00176      7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1239 RYQEkgsQLQERWHRVIAQLEIRQSELESIQEVLGDYRACHgTLIKWIEETTAQQEMMKPGQAEDSrvLSEQLSQQTALF 1318
Cdd:cd00176     79 ERLE---ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELE 152
                          170       180
                   ....*....|....*....|
gi 2020023496 1319 AEIERNQTKLDQCQKFSQQY 1338
Cdd:cd00176    153 EELEAHEPRLKSLNELAEEL 172
 
Name Accession Description Interval E-value
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
187-293 1.84e-71

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: 235.71  E-value: 1.84e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  187 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 266
Cdd:cd21240      1 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  267 DAEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
40-176 6.12e-69

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: 228.44  E-value: 6.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   40 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddv 119
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL-------------------------------- 48
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 176
Cdd:cd21188     49 PRERGRMRFHRLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-292 5.08e-40

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 161.26  E-value: 5.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   36 ADERDRVQKKTFTKWVNKHLMKV-RKHINDLYEDLRDGHNLISLLEVLSGIKLEpaglktlrlvsmpswchTNNeeqaee 114
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAG-----------------EYN------ 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  115 ddddvprEKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIyisGESGDMSAKEK 194
Cdd:COG5069     60 -------ETPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI---NEEGELTKHIN 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  195 LLLWTQKVTAGY-TGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN--RENLEQAFEVAER-LGVTRLLDAED 270
Cdd:COG5069    130 LLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkALNNFQAFENANKvIGIARLIGVED 209
                          250       260
                   ....*....|....*....|...
gi 2020023496  271 V-DVPSPDEKSVITYVSSIYDAF 292
Cdd:COG5069    210 IvNVSIPDERSIMTYVSWYIIRF 232
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7221-7296 7.06e-37

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


Pssm-ID: 128539  Cd Length: 73  Bit Score: 135.65  E-value: 7.06e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496  7221 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7296
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
7223-7297 5.91e-35

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


Pssm-ID: 460480  Cd Length: 69  Bit Score: 129.64  E-value: 5.91e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 7223 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 7297
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6326-6542 2.41e-31

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.87  E-value: 2.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6326 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 6405
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6406 RLEAMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 6485
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6486 KEETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHVVSSKMEERKSKLEEAL 6542
Cdd:cd00176    158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
953-1030 1.24e-30

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


Pssm-ID: 465730  Cd Length: 78  Bit Score: 117.70  E-value: 1.24e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  953 ISWNYLRKDLDLVQTWNLEKLRSSAPGECHQIMKNLQAHYEDFLQDSRDSVLFSVADRLRLEEEVEACKARFQHLMKS 1030
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6766-6978 1.84e-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: 122.55  E-value: 1.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6766 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6846 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 6925
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 6926 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 6978
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6547-6761 1.85e-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: 119.47  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6547 EFQNSLQEFINWLTLAEQSLNIASPPSlILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 6626
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6627 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 6706
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 6707 PVYDTTIRTGRALKEKtLLPEDSQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 6761
Cdd:cd00176    160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6106-6323 1.25e-25

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 108.69  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6106 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 6185
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6186 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQAMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 6265
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 6266 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 6323
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5343-5556 3.78e-23

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 101.37  E-value: 3.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5343 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 5422
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5423 ESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 5502
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5503 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLDQAL 5556
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
189-294 2.27e-22

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: 95.43  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYT-GIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTR 264
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKkLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2020023496  265 -LLDAEDVDvpSPDEKSVITYVSSIYDAFPK 294
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
852-918 3.50e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 93.10  E-value: 3.50e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  852 QLKPRSpdhvLKNT--ISVKAVCDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCFLIP 918
Cdd:pfam17902    1 PLKQRR----SPVTrpIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
193-288 8.86e-22

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: 93.53  E-value: 8.86e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   193 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR----ENLEQAFEVAERLGVTR-LLD 267
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVvLFE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496   268 AEDVDVPSPDEKSVITYVSSI 288
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5888-6104 6.96e-21

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 94.82  E-value: 6.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5888 QFWETYEELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQ 5967
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5968 KAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEpMLETLENLSSRLrMPPLIPAEVDKIRECISDNKSATVELEKLQP 6047
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6048 SFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 6104
Cdd:cd00176    161 RLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
45-174 2.05e-18

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: 83.90  E-value: 2.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496    45 KTFTKWVNKHLMK-VRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAGLKtlrlvsmpswchtnneeqaeeddddvpreK 123
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----------------------------A 51
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2020023496   124 GRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGnPKLTLGLIWTIILH 174
Cdd:smart00033   52 SLSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
42-177 3.55e-18

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: 83.49  E-value: 3.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHL--MKVRKHINDLYEDLRDGHNLISLLEvlsgiKLEPAGLKtlrlvsmpswchtnneeqaeeddddv 119
Cdd:pfam00307    2 ELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLN-----KLAPGLVD-------------------------- 50
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQ-VKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:pfam00307   51 KKKLNKSEFDKLENINLALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4688-4902 1.11e-17

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 85.58  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4688 YQELLQDLSEKVRAVGQRLSVQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 4767
Cdd:cd00176      9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4768 ETVALPLQGLEDLAADRINRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHS 4847
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 4848 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 4902
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
6328-6429 4.50e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 77.37  E-value: 4.50e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6328 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 6407
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 2020023496  6408 EAMNQCWESVLQKTEEREQQLQ 6429
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3878-4106 1.52e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 79.41  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3878 ELQKFLQDHKEFESWLERSEKELENMHkGGSSPETLPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDmensfkEGKEP 3957
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3958 SEIgnlVKDKLKDATERYTALHSKCTRLGSHLNMLLgQYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLA 4037
Cdd:cd00176     74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLK 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 4038 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAI 4106
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
677-866 2.50e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  677 LHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYS 756
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  757 AAVQSQLQWMKQLCLCVEQHVKENTAYFQFFSDARELESFLRNLQDSIKrkySCDHNTSLSRLEDLLQDSMDEKEQLIQS 836
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2020023496  837 KSSVASLVGRSKTIVQLKPRSPDHVLKNTI 866
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5778-5990 6.66e-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: 74.40  E-value: 6.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5778 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 5857
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5858 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEH 5937
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5938 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYQKAENMYAQIKEEVRQRALALDEA 5990
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4463-4682 1.29e-13

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4463 EEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTyPNSQEAENW 4542
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIE-EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4543 KKIQEELNSRWERATEVTVARQRQLEESASHLACFQAAEsQLRPWLMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 4622
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4623 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAI 4682
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
6766-6866 1.78e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 1.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6766 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  6846 ELSTRWDTVCKLSVSKQSRLE 6866
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1765-1800 3.81e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.58  E-value: 3.81e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2020023496 1765 LLEAQLFAGGIVDPRTGHRLTVEEAVRHNLIDQDMA 1800
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETA 36
SPEC smart00150
Spectrin repeats;
6656-6758 6.02e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.13  E-value: 6.02e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6656 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDSQKLDNF 6735
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 2020023496  6736 LGEVRDKWDTVCGKSVERQHKLE 6758
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4877-5807 6.62e-13

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: 76.63  E-value: 6.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4877 LVELKNHWEELskktaDRQSRlkdcmqKAQKYQwhvedlvpwiedckakmsELRVTLDPVQLESSLLRSKAmlnEVEKRR 4956
Cdd:TIGR02168  195 LNELERQLKSL-----ERQAE------KAERYK------------------ELKAELRELELALLVLRLEE---LREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4957 SLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAK 5030
Cdd:TIGR02168  243 ELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5031 HQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVAQQEFLEvkqRVNSG 5110
Cdd:TIGR02168  323 AQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5111 CVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAIGRDtdsLQSQIEDVRLFLNKIHVLKLDIEASEAECRHMLEEE 5190
Cdd:TIGR02168  388 VAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5191 GTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLndattaAEEAEALQWVVGTEVEIINqqlad 5270
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELIS----- 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5271 fkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW----------NTLNKKVAQRIAQLQEALL 5339
Cdd:TIGR02168  531 --------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLG 602
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5340 HCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiqeqkllqrlLDDRKATVDML------QAEG 5403
Cdd:TIGR02168  603 VAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT------------LDGDLVRPGGVitggsaKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5404 GRIAQSAELADREKitgQLESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSE-PVGTQTA 5482
Cdd:TIGR02168  671 SILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaEVEQLEE 747
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5483 KIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDSLQARYSEIQDRCcrkaALLDQALSNARlf 5562
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELR-- 809
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5563 gedevevlnwlAEVEDKLSSVFVKDFKQDVLHRQHADHLALNEEIVNRKKNV-DQAIKNGQALLKQTTGEEVLliQEKLD 5641
Cdd:TIGR02168  810 -----------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsEDIESLAAEIEELEELIEEL--ESELE 876
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5642 GIktryaditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAtsggqsptgeqipQFQQRQKELKKEVMEHRL 5721
Cdd:TIGR02168  877 AL-----------LNERASLEEALALL---RSELEELSEELRELESKRS-------------ELRRELEELREKLAQLEL 929
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5722 VLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYeqaadaelawVAETKRKLMAL 5801
Cdd:TIGR02168  930 RLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKEL 984

                   ....*.
gi 2020023496 5802 GPIRLE 5807
Cdd:TIGR02168  985 GPVNLA 990
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6328-6429 1.55e-12

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: 67.34  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6328 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 6407
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
                           90       100
                   ....*....|....*....|..
gi 2020023496 6408 EAMNQCWESVLQKTEEREQQLQ 6429
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4323-4570 4.01e-12

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.40  E-value: 4.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4323 QLDEFRKLVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTLVEEINCKGTSLenlimeitapdsqg 4402
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4403 ktgsilpsvgssvgsVNGYHTCKDltEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHkEANSVLQWLESKEEV 4482
Cdd:cd00176     67 ---------------IEEGHPDAE--EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4483 LKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIqEELNSRWERATEVTVA 4562
Cdd:cd00176    129 LASEDLGKDL---ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL-EELNERWEELLELAEE 204

                   ....*...
gi 2020023496 4563 RQRQLEES 4570
Cdd:cd00176    205 RQKKLEEA 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3581-4345 6.33e-12

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: 73.17  E-value: 6.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3581 LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRttqqdlsaLQKNQSDLKDLQDD 3660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3661 IQNRATSFATVVKDIEGFMEENQTKLSPR-----ELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSK 3735
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3736 AAKELAENKKKIDALldwvtsvgssggqlltnlpgMEQLsgaslekgaldttdgymgvnqapEKLDKQCEMMKARHQELL 3815
Cdd:TIGR02168  384 LRSKVAQLELQIASL--------------------NNEI-----------------------ERLEARLERLEDRRERLQ 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3816 SQQQnfilatqsaqafldQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLER 3895
Cdd:TIGR02168  421 QEIE--------------ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3896 SEKELenmhkggsspETLPSLLKRQGSFSEDVIshkgdlrfvtisgqkvldmeNSFKEGKEPSEIGNLVKDKLKdATERY 3975
Cdd:TIGR02168  487 LQARL----------DSLERLQENLEGFSEGVK--------------------ALLKNQSGLSGILGVLSELIS-VDEGY 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3976 TAlhSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEANVEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEK 4055
Cdd:TIGR02168  536 EA--AIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4056 LQK----------VARDI---MEIEGEPAPDHRHVQETTDSILSHF-------------QSLSYSLAERSSLLQKAIAQS 4109
Cdd:TIGR02168  614 LRKalsyllggvlVVDDLdnaLELAKKLRPGYRIVTLDGDLVRPGGvitggsaktnssiLERRREIEELEEKIEELEEKI 693
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4110 QSVQESLESLLQSIGEVEQNLEGKQV--------SSLSSGVIQEALATNMKLKQDIARQK---SSLEATREMVTRFMETA 4178
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLEEA 773
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4179 DSTTAAVLQgKLAEVSQRFEQLCLQQQEKESSLKKLlpQAEMFEH------LSGKLQQFMENKSRMLASGNQPDQDITHF 4252
Cdd:TIGR02168  774 EEELAEAEA-EIEELEAQIEQLKEELKALREALDEL--RAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4253 FQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVR 4332
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
                          810
                   ....*....|...
gi 2020023496 4333 TFQKWLKETEGSI 4345
Cdd:TIGR02168  926 QLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4094-4835 3.27e-11

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: 70.86  E-value: 3.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4094 SLAERSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLEGKQVSSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 4173
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4174 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLAsgnQPDQDITHFF 4253
Cdd:TIGR02168  324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA---QLELQIASLN 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4254 QQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 4333
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4334 FQKWLKETEGSIPPTETSMSakELEKQIEHLKSLLDdwaskgtlveeinckgtslenlimeitapdSQGKTGSILPSVGS 4413
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQE--NLEGFSEGVKALLK------------------------------NQSGLSGILGVLSE 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4414 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGvlherqeSLQAILNRMEEVHKEANSVLQWLESKEE---VLKSMDAMS 4490
Cdd:TIGR02168  528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4491 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIQEE-----------LNSRW------ 4553
Cdd:TIGR02168  586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4554 ERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKE----LMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 4629
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRkeleELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4630 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQR 4705
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4706 LSV----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELS---VLIGEQY-------------------- 4758
Cdd:TIGR02168  826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELEselEALLNERasleealallrseleelsee 902
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4759 -------------LKDELKKRLETVALPLQGLEdlaaDRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAK 4825
Cdd:TIGR02168  903 lreleskrselrrELEELREKLAQLELRLEGLE----VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-----RR 973
                          810
                   ....*....|
gi 2020023496 4826 LERLQSQLQE 4835
Cdd:TIGR02168  974 LKRLENKIKE 983
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7146-7216 9.43e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 9.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 7146 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 7216
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7146-7208 1.60e-10

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 59.87  E-value: 1.60e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 7146 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 7208
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5559-5774 2.43e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.00  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5559 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 5638
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5639 KLDGIKTRYADITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELAtSGGQSPTGEQIPQFQQRQKELKKEVME 5718
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 5719 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 5774
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
5343-5444 3.68e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 3.68e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  5343 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 5422
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 2020023496  5423 ESLESRWTELLSKAAARQKQLE 5444
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4796-4899 3.79e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 3.79e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4796 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 4875
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 2020023496  4876 QLVELKNHWEELSKKTADRQSRLK 4899
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6218-6320 5.12e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 5.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6218 QYQDTLQAMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 6297
Cdd:smart00150    2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 2020023496  6298 LTELKHLWENLGEKIAHRQHKLE 6320
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4796-4900 1.63e-09

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 58.48  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4796 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 4875
Cdd:pfam00435    4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
                           90       100
                   ....*....|....*....|....*
gi 2020023496 4876 QLVELKNHWEELSKKTADRQSRLKD 4900
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
5888-5988 2.04e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.11  E-value: 2.04e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  5888 QFWETYEELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQ 5967
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  5968 KAENMYAQIKEEVRQRALALD 5988
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2497-2535 4.01e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 4.01e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2497 LLTKQVVDGGIIHHISGMRLSVDNAFRHGLIGEDLAEKL 2535
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
EF-hand_7 pfam13499
EF-hand domain pair;
7144-7207 1.92e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 7144 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 7207
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4460-4569 4.96e-08

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 4.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4460 NRMEEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 4539
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 2020023496 4540 ENWKKiQEELNSRWERATEVTVARQRQLEE 4569
Cdd:pfam00435   77 EIQER-LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6766-6867 6.39e-08

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 6.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6766 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 2020023496 6846 ELSTRWDTVCKLSVSKQSRLEQ 6867
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3486-3722 6.58e-08

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.07  E-value: 6.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3486 QLEGRLQDLRAWVGNKNLILNSKGSNSeiDVDSLNLCLQQYEDLKQPMAERKAQLDALAFDIQFFISEHAQDLSPQQNRq 3565
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3566 mlrlLNELQRSFQDILEQTAAQVDALQGHLQQMEQealvktlqkqqntcHQQLEDLCSWVGQAERALAGHQgrtTQQDLS 3645
Cdd:cd00176     81 ----LEELNQRWEELRELAEERRQRLEEALDLQQF--------------FRDADDLEQWLEEKEAALASED---LGKDLE 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 3646 ALQKNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENQtklsPRELTALREKLHQAKEQYEALQEETRVAQKELEEA 3722
Cdd:cd00176    140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1574-1612 1.05e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 51.17  E-value: 1.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1574 LLESQVIMSGLIAPETGENLSLEEGIARNLINPQMYQQL 1612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1764-1800 1.48e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 50.94  E-value: 1.48e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2020023496  1764 RLLEAQLFAGGIVDPRTGHRLTVEEAVRHNLIDQDMA 1800
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2683-2721 1.62e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 50.79  E-value: 1.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2683 VLEAQANTGGIIDTATGKRLTLASALEEKLVDENMVRII 2721
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5343-5445 2.86e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5343 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSaELADREKITGQL 5422
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 2020023496 5423 ESLESRWTELLSKAAARQKQLED 5445
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3995-4103 2.89e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3995 QYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 4074
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKE---ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
                           90       100
                   ....*....|....*....|....*....
gi 2020023496 4075 RHVQETTDSILSHFQSLSYSLAERSSLLQ 4103
Cdd:pfam00435   76 EEIQERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
4463-4568 3.70e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 3.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4463 EEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 4542
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 2020023496  4543 KKIQEELNSRWERATEVTVARQRQLE 4568
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3551-3901 4.03e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3551 ISEHAQDLSPQQNRQMLRLLNELQRSFQDI--LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQA 3628
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELkeAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3629 ERALAGHQGRTTQQDLS----ALQKNQSDLKDLQDDIQNRATSFATVVKDIEgfMEENQTKLspreltALREKLHQAKEQ 3704
Cdd:COG4717    129 PLYQELEALEAELAELPerleELEERLEELRELEEELEELEAELAELQEELE--ELLEQLSL------ATEEELQDLAEE 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3705 YEALQEETRVAQKELEEAVT--SALQQETEKSKAAKELAENKKKIDALLDWVTSVgssGGQLLTNLPGMEQLSGASLEKG 3782
Cdd:COG4717    201 LEELQQRLAELEEELEEAQEelEELEEELEQLENELEAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTIAG 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3783 ALDTTDGYMGVnqAPEKLDKQCEMMKARHQELLSQQQNFILATQSAQAFLDQHG--HNLTPEEQQMLQQKLGELKEQYSt 3860
Cdd:COG4717    278 VLFLVLGLLAL--LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLR- 354
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2020023496 3861 SLAQSEAELkQVQTLQDELQKFLQ-----DHKEFESWLERSEKELE 3901
Cdd:COG4717    355 EAEELEEEL-QLEELEQEIAALLAeagveDEEELRAALEQAEEYQE 399
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6656-6759 6.99e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.17  E-value: 6.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6656 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDSQKLDNF 6735
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE--GHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 2020023496 6736 LGEVRDKWDTVCGKSVERQHKLEE 6759
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
6988-7112 1.72e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6988 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 7066
Cdd:smart00150    7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 2020023496  7067 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 7112
Cdd:smart00150   78 ----------------------RLEELNERWEELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5371-5934 2.50e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5371 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLESLESRWTELLSKAAARQKQLEDIL-VL 5449
Cdd:COG1196    214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5450 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 5523
Cdd:COG1196    291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5524 QGVLSEKIDSLQARYSEIQDRCCRKAALLDQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQHADHLAL 5603
Cdd:COG1196    371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5604 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYADIT---------VTSSKALRTLEQARQLATKFQst 5674
Cdd:COG1196    451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5675 yeELTGWLREVEEELATSGG---QSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 5746
Cdd:COG1196    528 --VLIGVEAAYEAALEAALAaalQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5747 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 5826
Cdd:COG1196    606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5827 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 5906
Cdd:COG1196    685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
                          570       580
                   ....*....|....*....|....*...
gi 2020023496 5907 IAQLPSPAIDHEQLRQQQEEMRQLRESI 5934
Cdd:COG1196    752 ALEELPEPPDLEELERELERLEREIEAL 779
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
3524-4200 3.67e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3524 QQYEDLKQPMAERKAQLDALAfDIQFFISEHAQDLSPQQNRQMLRLlnELQRSF-QDILEQTAAQVDAL-------QGHL 3595
Cdd:pfam15921  110 QSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQLQNTVHEL--EAAKCLkEDMLEDSNTQIEQLrkmmlshEGVL 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3596 QQME------QEALVKTLQKQQNTCHQQLEDLCSWVGQAERALaghqgrttQQDLSALQKN----QSDLKDLQDDIQNRA 3665
Cdd:pfam15921  187 QEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILREL--------DTEISYLKGRifpvEDQLEALKSESQNKI 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3666 TSFATVVKD-IEGFMEENQTklsprELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQ----ETEKSKAAKEL 3740
Cdd:pfam15921  259 ELLLQQHQDrIEQLISEHEV-----EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQlsdlESTVSQLRSEL 333
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3741 AENKK----KIDALLDWVTSVGSSGGQLLTNLPGMEQlsgaslEKGALDttdgymgvnqapEKLDKQCEMMKARHQEL-L 3815
Cdd:pfam15921  334 REAKRmyedKIEELEKQLVLANSELTEARTERDQFSQ------ESGNLD------------DQLQKLLADLHKREKELsL 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3816 SQQQNFILATQ-SAQAFLDQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLE 3894
Cdd:pfam15921  396 EKEQNKRLWDRdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE 475
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3895 RSEKELENMHKGGSSPETlpsllkrqgsfSEDVIShkgdlrfvtisgqkvlDMENSFKEgkepseignlvKDKLKDATer 3974
Cdd:pfam15921  476 MLRKVVEELTAKKMTLES-----------SERTVS----------------DLTASLQE-----------KERAIEAT-- 515
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3975 ytalHSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEA-NVEKLLSDTVASdpgVLQEQLATTKQL--QEELAEHQV 4051
Cdd:pfam15921  516 ----NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDKVIE---ILRQQIENMTQLvgQHGRTAGAM 588
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4052 PVEKLQ---------------KVARD-----IMEIEGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAiaqsQS 4111
Cdd:pfam15921  589 QVEKAQlekeindrrlelqefKILKDkkdakIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV----KT 664
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4112 VQESLESLLQSIGEVEQNLEGKQvsslssgviQEALATNMKLKQDIARQKSSLEATREMVtRFMETADSTTAAVLQGKLA 4191
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFRNKS---------EEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHAMKVAMGMQK 734

                   ....*....
gi 2020023496 4192 EVSQRFEQL 4200
Cdd:pfam15921  735 QITAKRGQI 743
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3408-3750 4.07e-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: 54.29  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3408 ERELKDLTtlvsQELECVNQIIISQPQEvpaqlLKALEKDAKNLQKSLSSVSDTWNsRLLHFQNAVEIEKTKVLNQHTQL 3487
Cdd:TIGR02168  676 RREIEELE----EKIEELEEKIAELEKA-----LAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3488 EGRLQDLRAWVGNKNLILNSKGSNSEIDVDSLNLCLQQYEDLKQPMAERKAQLDALAfdiqffisehaQDLSPQQNRqmL 3567
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----------EALDELRAE--L 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3568 RLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTchQQLEDLCSWVGQAERALAGHQGRTTQQDLsAL 3647
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEE-AL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3648 QKNQSDLKDLQDDIQNratsfatvvkdiegfMEENQTKLSpRELTALREKLHQAKEQYEALQEE--------TRVAQKEL 3719
Cdd:TIGR02168  890 ALLRSELEELSEELRE---------------LESKRSELR-RELEELREKLAQLELRLEGLEVRidnlqerlSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2020023496 3720 EEAVTSALQQETEKSKAAKELAENKKKIDAL 3750
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1803-1841 7.62e-06

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.17  E-value: 7.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1803 ILIRQLQTGGIIDTVTGQRLTIDEAVSNDLVAAKIALVI 1841
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
581-675 1.37e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.32  E-value: 1.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   581 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYA---ETLGKLE 657
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEeieERLEELN 83
                            90
                    ....*....|....*...
gi 2020023496   658 TQYCKLKETSSFRMRHLQ 675
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3997-4103 1.45e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.32  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  3997 HQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEKLQKVARDIMEIEGEPAPDhrh 4076
Cdd:smart00150    1 QQFLRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--- 74
                            90       100
                    ....*....|....*....|....*..
gi 2020023496  4077 VQETTDSILSHFQSLSYSLAERSSLLQ 4103
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
678-770 1.70e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   678 HKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYSA 757
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2020023496   758 AVQSQLQWMKQLC 770
Cdd:smart00150   81 ELNERWEELKELA 93
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6218-6320 2.15e-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: 46.93  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6218 QYQDTLQAMFDWLDNTVIKLcTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 6297
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
                           90       100
                   ....*....|....*....|...
gi 2020023496 6298 LTELKHLWENLGEKIAHRQHKLE 6320
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5964-6493 3.41e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5964 EKYQKAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRmppLIPAEVDKIRECISDNKSATVELE 6043
Cdd:PRK03918   158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN---EISSELPELREELEKLEKEVKELE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6044 KLQPSFEALKRRGEELIGRSQGADKDLaaKEIQD----------KLDQMVFFWEDIKARAEEREI------KFLDVLELA 6107
Cdd:PRK03918   235 ELKEEIEELEKELESLEGSKRKLEEKI--RELEErieelkkeieELEEKVKELKELKEKAEEYIKlsefyeEYLDELREI 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6108 EKfwyDMAALLTTIKDTQDIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLifacGETEKPEVRKS 6187
Cdd:PRK03918   313 EK---RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL----ERLKKRLTGLT 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6188 IDEMNNAWENLNKtwkeRLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIKL----CTMPPVGTDLnTVKDQLNEMKEFKVE 6263
Cdd:PRK03918   386 PEKLEKELEELEK----AKEEIEEEISKITARIGELKKEIKELKKAIEELkkakGKCPVCGREL-TEEHRKELLEEYTAE 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6264 VYQQQIEMEKLNHQgELMLKKATDETDRDIIREP-LTELKHLWENLGEKiahrQHKLEGallalgqfqHALEELMSWLTH 6342
Cdd:PRK03918   461 LKRIEKELKEIEEK-ERKLRKELRELEKVLKKESeLIKLKELAEQLKEL----EEKLKK---------YNLEELEKKAEE 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6343 TEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNEL---LESSAGDDASSLRSRLEAMNQCW----- 6414
Cdd:PRK03918   527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeLEELGFESVEELEERLKELEPFYneyle 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6415 ----ESVLQKTEEREQQLQSTLQQAQgfhSEIEDFLLELTRMESQLSASKPTGGlPETAREQLDTHMELYSQLKAKEETY 6490
Cdd:PRK03918   607 lkdaEKELEREEKELKKLEEELDKAF---EELAETEKRLEELRKELEELEKKYS-EEEYEELREEYLELSRELAGLRAEL 682

                   ...
gi 2020023496 6491 NQL 6493
Cdd:PRK03918   683 EEL 685
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2287-2325 3.74e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 44.24  E-value: 3.74e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2287 VLSAQLLDGGIFHEQTGQKLLLNEAISRGIVPSHTAVKL 2325
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1651-1689 5.27e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 5.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1651 ILEAHLATGGFSLSPSENCINLEEAFHQGLISAWLHSVL 1689
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
4645-5143 7.16e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 7.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4645 DVSLSTSQVQKELQSINQKwvELTDKLNSRSSQIDQAIVKSTQYQEllqdlsEKVRAVGQRLSVQSAIstqpEAVKQQLE 4724
Cdd:PRK02224   184 DQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEE------QREQARETRDEADEVL----EEHEERRE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4725 ETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQY-----LKDELKKRLETValplqGLEDLAADRINRLQAALASTQqfq 4799
Cdd:PRK02224   252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRerleeLEEERDDLLAEA-----GLDDADAEAVEARREELEDRD--- 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4800 qmfDELRTWLDD-KQSQQAKNCPIsaklERLQSQLQENEEFQKSLNQHSGSYEVIVAEGEslllsvppgEEKRTLQNQLV 4878
Cdd:PRK02224   324 ---EELRDRLEEcRVAAQAHNEEA----ESLREDADDLEERAEELREEAAELESELEEAR---------EAVEDRREEIE 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4879 ELKNHWEELSKKTADRQSRLKDCmqkaqkyQWHVEDLVPWIEDCKAKMSELRVTLDPVQlessllrskamlNEVEKRRSL 4958
Cdd:PRK02224   388 ELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELREREAELEATLRTAR------------ERVEEAEAL 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4959 LEILN--SAADILINSSEADEDGIRDEKAGinqNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAkhqleif 5036
Cdd:PRK02224   449 LEAGKcpECGQPVEGSPHVETIEEDRERVE---ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR------- 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5037 dalgsqacsnKNLEKLRAQQ-EVLQALEPQVDYLRNFTQGLVEDAPDGSDASQllhQAEVAQQEFLEVKQRVNSGCVMME 5115
Cdd:PRK02224   519 ----------EDLEELIAERrETIEEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELK 585
                          490       500
                   ....*....|....*....|....*...
gi 2020023496 5116 NKLEGIGqfhcRVREMFSQLADLDDELD 5143
Cdd:PRK02224   586 ERIESLE----RIRTLLAAIADAEDEIE 609
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5894-5989 7.17e-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: 45.39  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5894 EELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQKAENMY 5973
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
                           90
                   ....*....|....*.
gi 2020023496 5974 AQIKEEVRQRALALDE 5989
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4903-5007 7.39e-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: 45.39  E-value: 7.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4903 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRD 4982
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 2020023496 4983 EKAGINQNMDAVTEELQAKTGSLEE 5007
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PLEC smart00250
Plectin repeat;
2681-2718 1.24e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 1.24e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2020023496  2681 LKVLEAQANTGGIIDTATGKRLTLASALEEKLVDENMV 2718
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5879-6109 2.39e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5879 LERAQVLVNQFWETYEELSPWIEETRALIAQLPSPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 5958
Cdd:PRK03918   185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5959 GEMVEEKYQKAENMYAQIKE--EVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRmpplipaevdKIRECISDNK 6036
Cdd:PRK03918   265 EERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----------GIEERIKELE 334
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 6037 SATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 6109
Cdd:PRK03918   335 EKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2401-2432 3.91e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 41.16  E-value: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2401 ILERQVVTGGIIDLKRGKKVSVTLASTLGLVD 2432
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLID 32
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4547-5106 7.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4547 EELNSRWERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKELmmgvlgplsidpnMLNAQKQQVQFMLKEFEARR 4626
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------------ELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4627 QQHEQLNEAAQgiltgpgDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEK-VRAVGQR 4705
Cdd:COG1196    302 QDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlLEAEAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4706 LSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDELKKRLETVALPLQGLEDLAADRI 4785
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEELEEALAELEEEEEEEEEALEEAAE 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4786 NRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVP 4865
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4866 PGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQKYQWHVEDLVpwiedckakMSEL 4929
Cdd:COG1196    530 IGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGA---------IGAA 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4930 RVTLDPVQLESSLLRSKAMLNEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMT 5009
Cdd:COG1196    601 VDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5010 QRLREFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQL 5089
Cdd:COG1196    679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
                          570
                   ....*....|....*..
gi 2020023496 5090 LHQAEVAQQEFLEVKQR 5106
Cdd:COG1196    759 PPDLEELERELERLERE 775
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2363-2401 9.55e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.00  E-value: 9.55e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2363 VLMADKAISGVLDPRTQTLCSVKDAVTVGLLDKETATRI 2401
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
4906-5006 1.12e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4906 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 4985
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  4986 GINQNMDAVTEELQAKTGSLE 5006
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
4498-4835 1.13e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.10  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4498 VKAQAESNKAFLAELEQNSPKIQKVKEALAgllvtypnSQEA-ENWKKIQEELNSRWERATEVTVARQRQLEESASHLac 4576
Cdd:COG3096    315 LEELSARESDLEQDYQAASDHLNLVQTALR--------QQEKiERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL-- 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4577 fQAAESQLrpwlmeKELMMGVlgplsidpnmlnAQKQQVqfmLKEFEARRQQHEQLNEA---AQGILTGPgdvSLSTSQV 4653
Cdd:COG3096    385 -EAAEEEV------DSLKSQL------------ADYQQA---LDVQQTRAIQYQQAVQAlekARALCGLP---DLTPENA 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4654 QKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQ------------DLSEKVRAVGQRLSVQSAISTQPEAVKQ 4721
Cdd:COG3096    440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQRLQQLRA 519
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4722 QLeetseirSDLEQLDHEVKEAQTLCDELSVLIGEQY-LKDELKKRLETVALPLQGLEDLAADRINRLQAALASTQQFQQ 4800
Cdd:COG3096    520 QL-------AELEQRLRQQQNAERLLEEFCQRIGQQLdAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2020023496 4801 MFDELRT----WLDdkqSQQAkncpisakLERLQSQLQE 4835
Cdd:COG3096    593 RIKELAArapaWLA---AQDA--------LERLREQSGE 620
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4676-4897 1.19e-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: 45.53  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4676 SQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSVQSAISTQPEAVKQQLEET----SEIRSDLEQLDHEVKEAQTLCDELS 4751
Cdd:COG4942     17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarriRALEQELAALEAELAELEKEIAELR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4752 VLIGEQylKDELKKRLetVALPLQGLED-----LAADRINRLQAALASTQQF-QQMFDELRTWLDDKQSQQAKNCPISAK 4825
Cdd:COG4942     97 AELEAQ--KEELAELL--RALYRLGRQPplallLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALRAELEAE 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 4826 LERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPpgEEKRTLQNQLVELKNHWEELSKKTADRQSR 4897
Cdd:COG4942    173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLEAEAAAAAER 242
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2576-2607 1.44e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 39.62  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2576 EVQAFTGNFVDLISGQRLTLAEAKKEGLLTNE 2607
Cdd:pfam00681    3 EAQAATGGIIDPVTGERLSVEEAVKRGLIDPE 34
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
7379-7553 1.55e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7379 PSSPATPASGTKTSLQFSRC-YDKPWLVNSKAGTP-------IRDSHSPDLQLPTPEViPSSGSKLKRPTPTFHSSRTSL 7450
Cdd:PHA03307    84 SRSTPTWSLSTLAPASPAREgSPTPPGPSSPDPPPptpppasPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPAAV 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7451 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLL-ETQSACSD 7513
Cdd:PHA03307   163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGaSSSDSSSS 242
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2020023496 7514 TSESSAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 7553
Cdd:PHA03307   243 ESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
4650-5027 1.84e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4650 TSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSVQSA----ISTQPEAVKQQLEE 4725
Cdd:TIGR04523  227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4726 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRINRLQAALASTQQFQQMFD 4803
Cdd:TIGR04523  307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4804 ELRTWLDDKQS--QQAKNCPIS-AKLER-LQSQLQENEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 4878
Cdd:TIGR04523  371 EIEKLKKENQSykQEIKNLESQiNDLESkIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4879 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNE 4951
Cdd:TIGR04523  451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 4952 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVE 5027
Cdd:TIGR04523  531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
SPEC smart00150
Spectrin repeats;
3615-3720 2.85e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 2.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  3615 HQQLEDLCSWVGQAERALAGHQgrtTQQDLSALQKNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENqtklsPRELTAL 3694
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 2020023496  3695 REKLHQAKEQYEALQEETRVAQKELE 3720
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
mukB PRK04863
chromosome partition protein MukB;
4542-4845 4.01e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4542 WKKIQEELNSRWERATEVtvarQRQLEESASHLACFQAAESQLRPWLmekELMMgvlgplsidpNMLNAQKQ--QVQFML 4619
Cdd:PRK04863   295 LYTSRRQLAAEQYRLVEM----ARELAELNEAESDLEQDYQAASDHL---NLVQ----------TALRQQEKieRYQADL 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4620 KEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAI-----VKS--------- 4685
Cdd:PRK04863   358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVqalerAKQlcglpdlta 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4686 -------TQYQELLQDLSEKVRAVGQRLSVQSAISTQPEAVKQQL-------------EETSEIRSDLEQLDHEVKEAQT 4745
Cdd:PRK04863   438 dnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagevsrseawDVARELLRRLREQRHLAEQLQQ 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4746 LCDELSVLIGE-------QYLKDELKKRLETVALPLQGLEDLAADrinrLQAALASTQQFQQMFDELRTWLDDKQSQqak 4818
Cdd:PRK04863   518 LRMRLSELEQRlrqqqraERLLAEFCKRLGKNLDDEDELEQLQEE----LEARLESLSESVSEARERRMALRQQLEQ--- 590
                          330       340
                   ....*....|....*....|....*..
gi 2020023496 4819 ncpISAKLERLQSQLQENEEFQKSLNQ 4845
Cdd:PRK04863   591 ---LQARIQRLAARAPAWLAAQDALAR 614
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
5852-6109 4.69e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5852 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpspaidhEQLR 5921
Cdd:COG0497    116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5922 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYQKAENmYAQIKEEVRQRALALDE------ 5989
Cdd:COG0497    179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5990 --------AVSQSTQFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 6051
Cdd:COG0497    244 dllgqalrALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 6052 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 6109
Cdd:COG0497    311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
PLEC smart00250
Plectin repeat;
1807-1838 4.98e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 4.98e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2020023496  1807 QLQTGGIIDTVTGQRLTIDEAVSNDLVAAKIA 1838
Cdd:smart00250    7 QSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1850-1879 5.09e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 5.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2020023496 1850 GLLWPESGEILPITDALEQGIVSTELAHKI 1879
Cdd:pfam00681   10 GIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1159-1338 5.42e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.05  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1159 RSIQDAELLVKGYEIKLSQEEVVlADLSALEAHWSTLRHWLSDVKDKNSVFSVLDEEiakakvvAEQMSRLTPERNLDLE 1238
Cdd:cd00176      7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1239 RYQEkgsQLQERWHRVIAQLEIRQSELESIQEVLGDYRACHgTLIKWIEETTAQQEMMKPGQAEDSrvLSEQLSQQTALF 1318
Cdd:cd00176     79 ERLE---ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELE 152
                          170       180
                   ....*....|....*....|
gi 2020023496 1319 AEIERNQTKLDQCQKFSQQY 1338
Cdd:cd00176    153 EELEAHEPRLKSLNELAEEL 172
PLEC smart00250
Plectin repeat;
2285-2317 6.82e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.85  E-value: 6.82e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2020023496  2285 LNVLSAQLLDGGIFHEQTGQKLLLNEAISRGIV 2317
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
 
Name Accession Description Interval E-value
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
187-293 1.84e-71

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: 235.71  E-value: 1.84e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  187 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 266
Cdd:cd21240      1 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  267 DAEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
40-176 6.12e-69

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: 228.44  E-value: 6.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   40 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddv 119
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL-------------------------------- 48
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 176
Cdd:cd21188     49 PRERGRMRFHRLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
34-185 1.95e-68

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: 227.95  E-value: 1.95e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   34 GRADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqae 113
Cdd:cd21236      9 RYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL-------------------------- 62
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  114 eddddvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 185
Cdd:cd21236     63 ------PREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
37-186 1.04e-64

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: 216.82  E-value: 1.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   37 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeedd 116
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKL----------------------------- 51
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  117 ddvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 186
Cdd:cd21237     52 ---PREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
190-293 9.83e-64

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: 213.41  E-value: 9.83e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 268
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKeFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 2020023496  269 EDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
37-186 1.97e-60

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: 204.49  E-value: 1.97e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   37 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeedd 116
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL----------------------------- 51
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  117 ddvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 186
Cdd:cd21235     52 ---PREKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
190-293 7.14e-60

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: 202.52  E-value: 7.14e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 DVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21239     81 DVDVSSPDEKSVITYVSSLYDVFP 104
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
189-293 9.38e-49

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: 170.59  E-value: 9.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  268 AEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
36-173 5.14e-45

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: 160.61  E-value: 5.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   36 ADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAGlktlrlvsmpswchtnneeqaeed 115
Cdd:cd21246     10 ADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPT------------------------ 65
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  116 dddvpreKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21246     66 -------KGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
190-292 4.82e-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: 157.19  E-value: 4.82e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLDA 268
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEqELGIAKLLDA 81
                           90       100
                   ....*....|....*....|....
gi 2020023496  269 EDVDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYYHYF 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
42-177 1.10e-42

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: 153.31  E-value: 1.10e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHLMKVRK-HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddvP 120
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKL--------------------------------K 49
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  121 REKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21186     50 PEKGRMRVHHLNNVNRALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
190-292 3.69e-42

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: 151.78  E-value: 3.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 268
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQkLGLTKLLDP 81
                           90       100
                   ....*....|....*....|....
gi 2020023496  269 EDVDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYYHYF 105
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
189-293 1.77e-40

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: 147.08  E-value: 1.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  268 AEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
190-295 4.18e-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: 146.30  E-value: 4.18e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 268
Cdd:cd21319      5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERqLGITKLLDP 84
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  269 EDVDVPSPDEKSVITYVSSIYDAFPKV 295
Cdd:cd21319     85 EDVFTENPDEKSIITYVVAFYHYFSKM 111
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-292 5.08e-40

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 161.26  E-value: 5.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   36 ADERDRVQKKTFTKWVNKHLMKV-RKHINDLYEDLRDGHNLISLLEVLSGIKLEpaglktlrlvsmpswchTNNeeqaee 114
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAG-----------------EYN------ 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  115 ddddvprEKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIyisGESGDMSAKEK 194
Cdd:COG5069     60 -------ETPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI---NEEGELTKHIN 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  195 LLLWTQKVTAGY-TGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN--RENLEQAFEVAER-LGVTRLLDAED 270
Cdd:COG5069    130 LLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkALNNFQAFENANKvIGIARLIGVED 209
                          250       260
                   ....*....|....*....|...
gi 2020023496  271 V-DVPSPDEKSVITYVSSIYDAF 292
Cdd:COG5069    210 IvNVSIPDERSIMTYVSWYIIRF 232
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
177-292 8.13e-39

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: 142.50  E-value: 8.13e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  177 ISDIYISGesgdMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 256
Cdd:cd21216      1 IQDISVEE----LSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2020023496  257 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21216     77 AEKhLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
38-177 2.42e-38

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: 141.36  E-value: 2.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeed 115
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKL---------------------------- 52
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  116 dddvPREKGRM--RFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21241     53 ----PCEKGRRlkRVHFLSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
27-173 2.24e-37

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: 138.58  E-value: 2.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   27 YWKRHARGRADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAGlktlrlvsmpswcht 106
Cdd:cd21193      1 FEKGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPN--------------- 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  107 nneeqaeeddddvpreKGRMRFHRLQNVQIALDFLKQrQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21193     66 ----------------RGRLRVQKIENVNKALAFLKT-KVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
23-173 3.11e-37

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: 139.01  E-value: 3.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   23 AGVLYWKRHARGRADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmps 102
Cdd:cd21318     19 TAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL--------------- 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  103 wchtnneeqaeeddddvPR-EKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21318     84 -----------------PKpTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7221-7296 7.06e-37

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


Pssm-ID: 128539  Cd Length: 73  Bit Score: 135.65  E-value: 7.06e-37
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496  7221 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7296
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
189-293 6.53e-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: 134.09  E-value: 6.53e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  268 AEDVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
26-173 2.46e-35

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: 133.26  E-value: 2.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   26 LYWKRHARGRADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswch 105
Cdd:cd21317     15 LFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQL------------------ 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  106 tnneeqaeeddddvPR-EKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21317     77 --------------PKpTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
189-294 4.10e-35

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: 131.91  E-value: 4.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLD 267
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEqELGISQLLD 82
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  268 AEDVDVPSPDEKSVITYVSSIYDAFPK 294
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYYHYFSK 109
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
7223-7297 5.91e-35

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


Pssm-ID: 460480  Cd Length: 69  Bit Score: 129.64  E-value: 5.91e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 7223 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 7297
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
38-177 7.26e-35

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: 131.15  E-value: 7.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeed 115
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKL---------------------------- 52
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  116 dddvPREKGRM--RFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21190     53 ----PIESGRVlqRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
186-295 1.60e-33

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: 127.87  E-value: 1.60e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  186 SGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTR 264
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKeLGLTK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2020023496  265 LLDAEDVDVPSPDEKSVITYVSSIYDAFPKV 295
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKM 111
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
40-173 3.13e-32

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: 123.27  E-value: 3.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   40 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddV 119
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL-------------------------------P 51
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21214     52 KPERGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
177-292 4.20e-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: 123.41  E-value: 4.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  177 ISDIyisGESGdMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 256
Cdd:cd21291      1 IADI---NEEG-LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2020023496  257 AER-LGVTRLLDAEDV-DVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21291     77 ASKeIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
189-286 5.24e-32

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: 123.02  E-value: 5.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLE 83
                           90
                   ....*....|....*....
gi 2020023496  268 AEDVDVPSPDEKSVITYVS 286
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
42-175 1.10e-31

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: 122.12  E-value: 1.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktLRLVSMPswchtnneeqaeeddddvpr 121
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESL-------GRYNKNP-------------------- 56
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  122 ekgRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 175
Cdd:cd21215     57 ---KMRVQKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6326-6542 2.41e-31

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.87  E-value: 2.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6326 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 6405
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6406 RLEAMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 6485
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6486 KEETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHVVSSKMEERKSKLEEAL 6542
Cdd:cd00176    158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
176-295 2.43e-31

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: 122.08  E-value: 2.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  176 QISDIYISGESG--DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQA 253
Cdd:cd21322      1 QIQVIKIETEDNreTRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2020023496  254 FEVAER-LGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFPKV 295
Cdd:cd21322     81 FNTAEQhLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKM 123
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
193-293 3.15e-31

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: 120.61  E-value: 3.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  193 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVA-ERLGVTRLLDAED 270
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2020023496  271 VDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
38-177 9.51e-31

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: 119.55  E-value: 9.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeed 115
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQL---------------------------- 52
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  116 dddvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21242     53 ----PREKGHNVFQCRSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
953-1030 1.24e-30

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


Pssm-ID: 465730  Cd Length: 78  Bit Score: 117.70  E-value: 1.24e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  953 ISWNYLRKDLDLVQTWNLEKLRSSAPGECHQIMKNLQAHYEDFLQDSRDSVLFSVADRLRLEEEVEACKARFQHLMKS 1030
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
37-177 1.27e-30

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: 119.26  E-value: 1.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   37 DERDRVQKKTFTKWVNKHLMKVRK-HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeed 115
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKL---------------------------- 52
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  116 dddvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21231     53 ----VKEKGSTRVHALNNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6766-6978 1.84e-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: 122.55  E-value: 1.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6766 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6846 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 6925
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 6926 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 6978
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
195-292 3.31e-30

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: 117.83  E-value: 3.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  195 LLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED-VD 272
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDmVA 85
                           90       100
                   ....*....|....*....|
gi 2020023496  273 VPSPDEKSVITYVSSIYDAF 292
Cdd:cd21253     86 LKVPDKLSILTYVSQYYNYF 105
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
190-295 3.37e-30

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: 117.89  E-value: 3.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 268
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
                           90       100
                   ....*....|....*....|....*..
gi 2020023496  269 EDVDVPSPDEKSVITYVSSIYDAFPKV 295
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6547-6761 1.85e-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: 119.47  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6547 EFQNSLQEFINWLTLAEQSLNIASPPSlILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 6626
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6627 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 6706
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 6707 PVYDTTIRTGRALKEKtLLPEDSQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 6761
Cdd:cd00176    160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
26-173 1.63e-28

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: 114.76  E-value: 1.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   26 LYWKRHARGRADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAglktlrlvsmpswch 105
Cdd:cd21316     37 LFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP--------------- 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  106 tnneeqaeeddddvprEKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 173
Cdd:cd21316    102 ----------------TKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
190-292 3.94e-28

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: 111.75  E-value: 3.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 DVDVPS-PDEKSVITYVSSIYDAF 292
Cdd:cd21198     81 DMVLLSvPDKLSVMTYLHQIRAHF 104
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
193-292 5.38e-28

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: 111.22  E-value: 5.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  193 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED- 270
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|..
gi 2020023496  271 VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEAF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6653-6869 1.23e-27

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 114.47  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6653 RAKQFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDSQKL 6732
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6733 DNFLGEVRDKWDTVCGKSVERQHKLEEALLFSgQFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKEL 6812
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 6813 GKRTGTVQVLKRSGRELIENSR-DDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQAL 6869
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
41-178 2.56e-27

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: 110.23  E-value: 2.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEpaglktlrlvsmpswcHTNneeqaeeddddvp 120
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFP----------------KFN------------- 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  121 rEKGRMRFHRLQNVQIALDFLKQRQ-VKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21311     65 -KRPTFRSQKLENVSVALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
175-298 3.55e-27

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: 109.79  E-value: 3.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  175 FQISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAF 254
Cdd:cd21290      2 FAIQDISVE----ETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2020023496  255 EVAER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAFPKVPEG 298
Cdd:cd21290     78 EVAEKyLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAFSGAQKA 123
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
41-175 5.25e-27

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: 108.72  E-value: 5.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPaglktlrlvsmpSWchtnneeqaeeddddvp 120
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKR------------SY----------------- 53
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496  121 REKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 175
Cdd:cd21183     54 NRRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
42-177 1.28e-26

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: 107.37  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAGLKTLrlvsmpswchtnneeqaeeddddvpr 121
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPL-------------------------- 57
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496  122 ekgrMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21227     58 ----NQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
190-292 6.22e-26

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: 105.64  E-value: 6.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21255     81 DmVLLPIPDKLIVMTYLCQLRAHF 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
42-177 6.96e-26

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: 105.48  E-value: 6.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHLMKVRK-HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddddvP 120
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSL--------------------------------P 49
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496  121 REKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21232     50 KERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
38-179 7.44e-26

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: 105.74  E-value: 7.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrLVSMPSWCHtnneeqaeed 115
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNL---------LQEYKPSSH---------- 61
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  116 dddvprekgrmRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 179
Cdd:cd21191     62 -----------RIFRLNNIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6106-6323 1.25e-25

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 108.69  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6106 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 6185
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6186 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQAMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 6265
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 6266 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 6323
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
177-292 1.35e-25

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: 105.19  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  177 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 256
Cdd:cd21289      1 IQDISVE----ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2020023496  257 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21289     77 AEKyLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
190-292 3.33e-25

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: 103.59  E-value: 3.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21199      8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPTTLTID 87
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21199     88 EmVSMERPDWQSVMSYVTAIYKHF 111
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
193-294 3.34e-25

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: 103.47  E-value: 3.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  193 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERV-QIQSNRENLEQAFEVAER-LGVTRLLDAE 269
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQhLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 2020023496  270 DVDVPSPDEKSVITYVSSIYDAFPK 294
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
177-297 6.49e-25

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: 103.24  E-value: 6.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  177 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 256
Cdd:cd21287      1 IQDISVE----ETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2020023496  257 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAFPKVPE 297
Cdd:cd21287     77 AEKyLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAFSGAQK 119
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
190-292 1.25e-24

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: 101.65  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 268
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELAdIAPLLEV 80
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  269 EDVDV--PSPDEKSVITYVSSIYDAF 292
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLYRHL 106
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
193-293 1.86e-24

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: 101.19  E-value: 1.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  193 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED 270
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2020023496  271 VDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
41-175 1.92e-24

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: 101.41  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKlepaglktlrlvsMPSWCHtnneeqaeeddddvp 120
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKR-------------MYKKYN--------------- 54
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496  121 rEKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 175
Cdd:cd21228     55 -KRPTFRQMKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
191-293 6.59e-24

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: 99.87  E-value: 6.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  191 AKEKLLLWTQKVTAGYtGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 269
Cdd:cd21245      4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQEsLGIPPLLEPE 82
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 DVDVPSPDEKSVITYVSSIYDAFP 293
Cdd:cd21245     83 DVMVDSPDEQSIMTYVAQFLEHFP 106
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
177-292 1.88e-23

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: 98.99  E-value: 1.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  177 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 256
Cdd:cd21288      1 IQDISVE----ETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2020023496  257 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21288     77 AEKhLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5343-5556 3.78e-23

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 101.37  E-value: 3.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5343 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 5422
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5423 ESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 5502
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5503 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLDQAL 5556
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
193-292 6.65e-23

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: 96.77  E-value: 6.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  193 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDV 271
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 2020023496  272 DVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
195-292 1.48e-22

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: 95.68  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  195 LLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED-VD 272
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETsLGIPALLDAEDmVT 84
                           90       100
                   ....*....|....*....|
gi 2020023496  273 VPSPDEKSVITYVSSIYDAF 292
Cdd:cd21197     85 MHVPDRLSIITYVSQYYNHF 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6218-6432 1.58e-22

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 99.44  E-value: 1.58e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6218 QYQDTLQAMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 6297
Cdd:cd00176      4 QFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6298 LTELKHLWENLGEKIAHRQHKLEGALLALgQFQHALEELMSWLTHTEELLDAQrPISGDPKVIEVELAKHHVLKNDVLAH 6377
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 6378 QATVETVNKAGNELLESSAGDDASSLRSRLEAMNQCWESVLQKTEEREQQLQSTL 6432
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
189-294 2.27e-22

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: 95.43  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYT-GIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTR 264
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKkLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2020023496  265 -LLDAEDVDvpSPDEKSVITYVSSIYDAFPK 294
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
41-178 2.96e-22

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: 95.87  E-value: 2.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglkTLRLVSMPSWchtnneeqaeeddddvp 120
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM------YRKYHPRPNF----------------- 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  121 rekgrmRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21310     72 ------RQMKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
852-918 3.50e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 93.10  E-value: 3.50e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  852 QLKPRSpdhvLKNT--ISVKAVCDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCFLIP 918
Cdd:pfam17902    1 PLKQRR----SPVTrpIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
190-292 6.26e-22

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: 94.15  E-value: 6.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21254     81 DmVLLAVPDKLTVMTYLYQIRAHF 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
193-288 8.86e-22

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: 93.53  E-value: 8.86e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   193 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR----ENLEQAFEVAERLGVTR-LLD 267
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVvLFE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496   268 AEDVDVPSPDEKSVITYVSSI 288
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
27-177 5.36e-21

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: 92.13  E-value: 5.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   27 YWKRHARGRADERDRVQKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEVLSGIKLEPaglktlrlvsmPSwc 104
Cdd:cd21247      5 YEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKngAKIEITDIYTELKDGIHLLRLLELISGEQLPR-----------PS-- 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  105 htnneeqaeeddddvpreKGRMRFHRLQNVQIALDFLKQR-QVKLVNIRNddITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21247     72 ------------------RGKMRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5888-6104 6.96e-21

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 94.82  E-value: 6.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5888 QFWETYEELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQ 5967
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5968 KAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEpMLETLENLSSRLrMPPLIPAEVDKIRECISDNKSATVELEKLQP 6047
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 6048 SFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 6104
Cdd:cd00176    161 RLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
191-294 2.61e-20

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: 89.54  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  191 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 269
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPE 80
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAFPK 294
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYYNHFSN 106
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
190-292 3.38e-20

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: 89.32  E-value: 3.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21257     88 EmMYTDRPDWQSVMQYVAQIYKYF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6871-7115 4.17e-20

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 92.51  E-value: 4.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6871 QAEVFRDTVHMLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIK 6950
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6951 HWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELlawiQWAETTLIQRDQEPIPQNIDRVKALIAEHQTFMEE 7030
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE----QWLEEKEAALASEDLGKDLESVEELLKKHKELEEE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7031 MTRKQPDVDRVTKtykrkniepTHAPFIEKSRSGGrkslsqptpppmpilsqSEAKNPRINQLSARWQQVWLLALERQRK 7110
Cdd:cd00176    155 LEAHEPRLKSLNE---------LAEELLEEGHPDA-----------------DEEIEEKLEELNERWEELLELAEERQKK 208

                   ....*
gi 2020023496 7111 LNDAL 7115
Cdd:cd00176    209 LEEAL 213
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
190-292 7.74e-20

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: 88.59  E-value: 7.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 269
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKSTLDIN 93
                           90       100
                   ....*....|....*....|....
gi 2020023496  270 D-VDVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21256     94 EmVRTERPDWQSVMTYVTAIYKYF 117
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
190-289 1.23e-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: 87.74  E-value: 1.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 268
Cdd:cd21259      1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80
                           90       100
                   ....*....|....*....|..
gi 2020023496  269 ED-VDVPSPDEKSVITYVSSIY 289
Cdd:cd21259     81 EDmVRMREPDWKCVYTYIQEFY 102
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
190-287 1.84e-19

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: 86.91  E-value: 1.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYtgiKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR-ENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEeLGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 2020023496  268 AEDVDVPSPDEKSVITYVSS 287
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
190-290 1.93e-19

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: 86.94  E-value: 1.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERL-GVTRLLDA 268
Cdd:cd21261      1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  269 EDVDV--PSPDEKSVITYVSSIYD 290
Cdd:cd21261     81 EDMMVmgRKPDPMCVFTYVQSLYN 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6434-6651 7.79e-19

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 89.04  E-value: 7.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6434 QAQGFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKAKEETYNQLLDKG-RLMLLSRDDSgsgSK 6512
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGeQLIEEGHPDA---EE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6513 TEQSVALLEQKWHVVSSKMEERKSKLEEALNLATEFQnSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANE 6592
Cdd:cd00176     77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 6593 VNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDAR 6651
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
190-290 1.31e-18

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: 84.71  E-value: 1.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 268
Cdd:cd21258      1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLAdCVPLVEV 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  269 EDVDV--PSPDEKSVITYVSSIYD 290
Cdd:cd21258     81 EDMMImgKKPDSKCVFTYVQSLYN 104
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
192-289 1.36e-18

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: 85.14  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  192 KEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDAED 270
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
                           90       100
                   ....*....|....*....|
gi 2020023496  271 -VDVPSPDEKSVITYVSSIY 289
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELY 102
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
194-292 1.95e-18

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: 84.32  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  194 KLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDV- 271
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEReFGIPPVTTGKEMa 87
                           90       100
                   ....*....|....*....|.
gi 2020023496  272 DVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYELF 108
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
189-292 1.96e-18

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: 84.23  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  189 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21251      4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKeFGISPIMT 83
                           90       100
                   ....*....|....*....|....*.
gi 2020023496  268 AEDV-DVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21251     84 GKEMaSVGEPDKLSMVMYLTQFYEMF 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
45-174 2.05e-18

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: 83.90  E-value: 2.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496    45 KTFTKWVNKHLMK-VRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAGLKtlrlvsmpswchtnneeqaeeddddvpreK 123
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----------------------------A 51
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2020023496   124 GRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGnPKLTLGLIWTIILH 174
Cdd:smart00033   52 SLSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
41-178 2.37e-18

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: 84.75  E-value: 2.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddDDVP 120
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM-----------------------------YRKY 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  121 REKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21309     67 HQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
42-177 3.55e-18

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: 83.49  E-value: 3.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   42 VQKKTFTKWVNKHL--MKVRKHINDLYEDLRDGHNLISLLEvlsgiKLEPAGLKtlrlvsmpswchtnneeqaeeddddv 119
Cdd:pfam00307    2 ELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLN-----KLAPGLVD-------------------------- 50
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  120 PREKGRMRFHRLQNVQIALDFLKQRQ-VKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:pfam00307   51 KKKLNKSEFDKLENINLALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
41-178 3.79e-18

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: 84.37  E-value: 3.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   41 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLepaglktlrlvsmpswchtnneeqaeeddDDVP 120
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKM-----------------------------HRKH 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  121 REKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21308     70 NQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5254-5447 5.53e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.35  E-value: 5.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5254 QWVVGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQ 5333
Cdd:cd00176     25 STDYGDDLESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE--IQERLEELNQRWEELRELAEERRQR 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5334 LQEALLHCGKFQDALEpLLSWLADTEELIANQKPPSAEYKvVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA 5413
Cdd:cd00176    102 LEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD 179
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2020023496 5414 DREKITGQLESLESRWTELLSKAAARQKQLEDIL 5447
Cdd:cd00176    180 ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4688-4902 1.11e-17

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 85.58  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4688 YQELLQDLSEKVRAVGQRLSVQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 4767
Cdd:cd00176      9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4768 ETVALPLQGLEDLAADRINRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHS 4847
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 4848 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 4902
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4796-5008 2.26e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4796 QQFQQMFDELRTWLDDKQSQQAKNCPISaKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 4875
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4876 QLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQwHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKR 4955
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 4956 RSLLEILNSAADILINSSEADEDGIRDEKA-GINQNMDAVTEELQAKTGSLEEM 5008
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLeELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
6328-6429 4.50e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 77.37  E-value: 4.50e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6328 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 6407
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 2020023496  6408 EAMNQCWESVLQKTEEREQQLQ 6429
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
194-292 7.71e-16

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: 76.84  E-value: 7.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  194 KLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDVD 272
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEReFGIPPVTTGKEMA 87
                           90       100
                   ....*....|....*....|.
gi 2020023496  273 -VPSPDEKSVITYVSSIYDAF 292
Cdd:cd21250     88 sAEEPDKLSMVMYLSKFYELF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5449-5665 1.05e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 79.80  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5449 LAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAkIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLS 5528
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5529 EKIDSLQARYSEIQDRCCRKAALLDQALSNARLFgEDEVEVLNWLAEVEDKLSSVFVKDFKQDVlHRQHADHLALNEEIV 5608
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 5609 NRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQAR 5665
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3878-4106 1.52e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 79.41  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3878 ELQKFLQDHKEFESWLERSEKELENMHkGGSSPETLPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDmensfkEGKEP 3957
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3958 SEIgnlVKDKLKDATERYTALHSKCTRLGSHLNMLLgQYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLA 4037
Cdd:cd00176     74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLK 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 4038 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAI 4106
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
190-292 3.23e-15

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: 75.08  E-value: 3.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLDA 268
Cdd:cd21196      3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAEnELGITPVVSA 82
                           90       100
                   ....*....|....*....|....
gi 2020023496  269 EDVdVPSPDEKSVITYVSSIYDAF 292
Cdd:cd21196     83 QAV-VAGSDPLGLIAYLSHFHSAF 105
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
194-286 1.61e-14

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: 73.87  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  194 KLLL-WTQKVTAGYtGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN-------------------------- 246
Cdd:cd21224      3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2020023496  247 ---------RENLEQAFEVAERLG-VTRLLDAEDVDVPSPDEKSVITYVS 286
Cdd:cd21224     82 lssellaneKRNFKLVQQAVAELGgVPALLRASDMSNTIPDEKVVILFLS 131
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
677-866 2.50e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.95  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  677 LHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYS 756
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  757 AAVQSQLQWMKQLCLCVEQHVKENTAYFQFFSDARELESFLRNLQDSIKrkySCDHNTSLSRLEDLLQDSMDEKEQLIQS 836
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2020023496  837 KSSVASLVGRSKTIVQLKPRSPDHVLKNTI 866
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
38-169 4.64e-14

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: 72.07  E-value: 4.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRvQKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnLIsLLEVLSgiKLEPAglktlrlvsMPSWCHTNNEeqaeeddd 117
Cdd:cd21300      4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDG--LI-LLQAYD--KVIPG---------SVNWKKVNKA-------- 58
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  118 dvPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIW 169
Cdd:cd21300     59 --PASAEISRFKAVENTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
192-290 5.30e-14

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: 71.22  E-value: 5.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  192 KEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN---RENLEQAFEVAERLGV--TRLL 266
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGLpeLDLF 80
                           90       100
                   ....*....|....*....|....
gi 2020023496  267 DAEDVdVPSPDEKSVITYVSSIYD 290
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5778-5990 6.66e-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: 74.40  E-value: 6.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5778 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 5857
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5858 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEH 5937
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5938 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYQKAENMYAQIKEEVRQRALALDEA 5990
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
581-779 7.82e-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: 7.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  581 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFH---TSYAETLGKLE 657
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdaEEIQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  658 TQYCKLKETSSFRMRHLQ---SLHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSL 734
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2020023496  735 QDTAELLSLENHPAKQtveaysAAVQSQLQWMKQLCLCVEQHVKE 779
Cdd:cd00176    166 NELAEELLEEGHPDAD------EEIEEKLEELNERWEELLELAEE 204
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4463-4682 1.29e-13

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4463 EEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTyPNSQEAENW 4542
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIE-EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4543 KKIQEELNSRWERATEVTVARQRQLEESASHLACFQAAEsQLRPWLMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 4622
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4623 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAI 4682
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3995-4211 1.36e-13

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3995 QYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 4074
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKE---ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4075 RHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLEsLLQSIGEVEQNLEgKQVSSLSSGVIQEALATNMKLK 4154
Cdd:cd00176     75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELE 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 4155 QDIARQKSSLEATREMVTRFMETADSTTAAVLQGKLAEVSQRFEQLCLQQQEKESSL 4211
Cdd:cd00176    153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
36-174 1.70e-13

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: 70.39  E-value: 1.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   36 ADERDrvqKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSgiKLEPAGLktlrlvsmpSWCHTNneeqaeed 115
Cdd:cd21219      1 EGSRE---ERAFRMWLNS--LGLDPLINNLYEDLRDG---LVLLQVLD--KIQPGCV---------NWKKVN-------- 53
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  116 dddvpREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILH 174
Cdd:cd21219     54 -----KPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC smart00150
Spectrin repeats;
6766-6866 1.78e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 1.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6766 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  6846 ELSTRWDTVCKLSVSKQSRLE 6866
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
43-175 1.93e-13

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: 69.92  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   43 QKKTFTKWVNKHL--MKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPAglktlrlvsmpswcHTNNEeqaeeddddvp 120
Cdd:cd21212      1 EIEIYTDWANHYLekGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGI--------------HSRPK----------- 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496  121 rekgrMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 175
Cdd:cd21212     56 -----TRAQKLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1765-1800 3.81e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.58  E-value: 3.81e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2020023496 1765 LLEAQLFAGGIVDPRTGHRLTVEEAVRHNLIDQDMA 1800
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETA 36
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6041-6213 5.33e-13

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 5.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6041 ELEKLQPSFEALKRRGEELIgrsqgADKDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEKFWyDMAALLTT 6120
Cdd:cd00176     48 ELAAHEERVEALNELGEQLI-----EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQW 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6121 IKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVRKSIDEMNNAWENLNK 6200
Cdd:cd00176    122 LEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
                          170
                   ....*....|...
gi 2020023496 6201 TWKERLEKLEDAM 6213
Cdd:cd00176    201 LAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
6656-6758 6.02e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.13  E-value: 6.02e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6656 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDSQKLDNF 6735
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 2020023496  6736 LGEVRDKWDTVCGKSVERQHKLE 6758
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4877-5807 6.62e-13

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: 76.63  E-value: 6.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4877 LVELKNHWEELskktaDRQSRlkdcmqKAQKYQwhvedlvpwiedckakmsELRVTLDPVQLESSLLRSKAmlnEVEKRR 4956
Cdd:TIGR02168  195 LNELERQLKSL-----ERQAE------KAERYK------------------ELKAELRELELALLVLRLEE---LREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4957 SLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAK 5030
Cdd:TIGR02168  243 ELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5031 HQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVAQQEFLEvkqRVNSG 5110
Cdd:TIGR02168  323 AQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5111 CVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAIGRDtdsLQSQIEDVRLFLNKIHVLKLDIEASEAECRHMLEEE 5190
Cdd:TIGR02168  388 VAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5191 GTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLndattaAEEAEALQWVVGTEVEIINqqlad 5270
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELIS----- 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5271 fkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW----------NTLNKKVAQRIAQLQEALL 5339
Cdd:TIGR02168  531 --------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLG 602
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5340 HCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiqeqkllqrlLDDRKATVDML------QAEG 5403
Cdd:TIGR02168  603 VAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT------------LDGDLVRPGGVitggsaKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5404 GRIAQSAELADREKitgQLESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSE-PVGTQTA 5482
Cdd:TIGR02168  671 SILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaEVEQLEE 747
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5483 KIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDSLQARYSEIQDRCcrkaALLDQALSNARlf 5562
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELR-- 809
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5563 gedevevlnwlAEVEDKLSSVFVKDFKQDVLHRQHADHLALNEEIVNRKKNV-DQAIKNGQALLKQTTGEEVLliQEKLD 5641
Cdd:TIGR02168  810 -----------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsEDIESLAAEIEELEELIEEL--ESELE 876
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5642 GIktryaditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAtsggqsptgeqipQFQQRQKELKKEVMEHRL 5721
Cdd:TIGR02168  877 AL-----------LNERASLEEALALL---RSELEELSEELRELESKRS-------------ELRRELEELREKLAQLEL 929
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5722 VLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYeqaadaelawVAETKRKLMAL 5801
Cdd:TIGR02168  930 RLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKEL 984

                   ....*.
gi 2020023496 5802 GPIRLE 5807
Cdd:TIGR02168  985 GPVNLA 990
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
45-178 7.16e-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: 68.80  E-value: 7.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   45 KTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEvlsgiKLEPaGLKTLRLVSMPswchtnneeqaeeddddvPREKG 124
Cdd:cd21298      9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYD-----KIKP-GVVDWSRVNKP------------------FKKLG 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  125 RMrFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21298     63 AN-MKKIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6328-6429 1.55e-12

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: 67.34  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6328 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 6407
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
                           90       100
                   ....*....|....*....|..
gi 2020023496 6408 EAMNQCWESVLQKTEEREQQLQ 6429
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4323-4570 4.01e-12

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.40  E-value: 4.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4323 QLDEFRKLVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTLVEEINCKGTSLenlimeitapdsqg 4402
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4403 ktgsilpsvgssvgsVNGYHTCKDltEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHkEANSVLQWLESKEEV 4482
Cdd:cd00176     67 ---------------IEEGHPDAE--EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4483 LKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIqEELNSRWERATEVTVA 4562
Cdd:cd00176    129 LASEDLGKDL---ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL-EELNERWEELLELAEE 204

                   ....*...
gi 2020023496 4563 RQRQLEES 4570
Cdd:cd00176    205 RQKKLEEA 212
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
190-295 5.65e-12

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: 65.48  E-value: 5.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQKVTAGytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLD 267
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
                           90       100
                   ....*....|....*....|....*...
gi 2020023496  268 AEDVDVPSPDEKSVITYVSSiydaFPKV 295
Cdd:cd21230     78 PEEIINPNVDEMSVMTYLSQ----FPKA 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3581-4345 6.33e-12

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: 73.17  E-value: 6.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3581 LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRttqqdlsaLQKNQSDLKDLQDD 3660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3661 IQNRATSFATVVKDIEGFMEENQTKLSPR-----ELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSK 3735
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3736 AAKELAENKKKIDALldwvtsvgssggqlltnlpgMEQLsgaslekgaldttdgymgvnqapEKLDKQCEMMKARHQELL 3815
Cdd:TIGR02168  384 LRSKVAQLELQIASL--------------------NNEI-----------------------ERLEARLERLEDRRERLQ 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3816 SQQQnfilatqsaqafldQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLER 3895
Cdd:TIGR02168  421 QEIE--------------ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3896 SEKELenmhkggsspETLPSLLKRQGSFSEDVIshkgdlrfvtisgqkvldmeNSFKEGKEPSEIGNLVKDKLKdATERY 3975
Cdd:TIGR02168  487 LQARL----------DSLERLQENLEGFSEGVK--------------------ALLKNQSGLSGILGVLSELIS-VDEGY 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3976 TAlhSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEANVEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEK 4055
Cdd:TIGR02168  536 EA--AIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4056 LQK----------VARDI---MEIEGEPAPDHRHVQETTDSILSHF-------------QSLSYSLAERSSLLQKAIAQS 4109
Cdd:TIGR02168  614 LRKalsyllggvlVVDDLdnaLELAKKLRPGYRIVTLDGDLVRPGGvitggsaktnssiLERRREIEELEEKIEELEEKI 693
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4110 QSVQESLESLLQSIGEVEQNLEGKQV--------SSLSSGVIQEALATNMKLKQDIARQK---SSLEATREMVTRFMETA 4178
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLEEA 773
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4179 DSTTAAVLQgKLAEVSQRFEQLCLQQQEKESSLKKLlpQAEMFEH------LSGKLQQFMENKSRMLASGNQPDQDITHF 4252
Cdd:TIGR02168  774 EEELAEAEA-EIEELEAQIEQLKEELKALREALDEL--RAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4253 FQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVR 4332
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
                          810
                   ....*....|...
gi 2020023496 4333 TFQKWLKETEGSI 4345
Cdd:TIGR02168  926 QLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4652-5500 2.18e-11

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: 71.63  E-value: 2.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4652 QVQKELQSINQKWVELTDKLNSRSSQID----QAiVKSTQYQELLQDLSEKVRAvgqrLSVQSaistqpeaVKQQLEETS 4727
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILNELERQLKslerQA-EKAERYKELKAELRELELA----LLVLR--------LEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4728 EIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKD-ELKKRLETvalpLQGLEDLAADRINRLQaalastqQFQQMFDELR 4806
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEE----LQKELYALANEISRLE-------QQKQILRERL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4807 TWLDDKQSQqakncpISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPpgEEKRTLQNQLVELKNHWEE 4886
Cdd:TIGR02168  312 ANLERQLEE------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--AELEELESRLEELEEQLET 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4887 LSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAA 4966
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4967 DILINSSEADEDGIRDEKAGINQnmdavteeLQAKTGSLEEMTQRLREFQESFKNIEKkvegAKHQLE-IFDALGSQACS 5045
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLK----NQSGLSgILGVLSELISV 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5046 NKNLEKlraqqEVLQALEPQVDYLrnftqgLVEDAPDGSDASQLLHQAEVAQQEFLEVK----QRVNSGCVMMENKLEGI 5121
Cdd:TIGR02168  532 DEGYEA-----AIEAALGGRLQAV------VVENLNAAKKAIAFLKQNELGRVTFLPLDsikgTEIQGNDREILKNIEGF 600
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5122 GQFHCRVREMFSQL-ADLDDELDGMgaigRDTDSLQSQIEDVRL--FLNKIHVLKLDIEASeaecRHML---EEEGTLDL 5195
Cdd:TIGR02168  601 LGVAKDLVKFDPKLrKALSYLLGGV----LVVDDLDNALELAKKlrPGYRIVTLDGDLVRP----GGVItggSAKTNSSI 672
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5196 LGLKRELEALNKQCGKLTER---GKARQEQLELTLGRVEDFYRKL-KGLNDATTAAEEAEALQWVVGTEVEIINQQLADF 5271
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKiaeLEKALAELRKELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5272 KMFQKEQVDPLQMKLQQVNGLGQGLIQSAGKdcdVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPL 5351
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5352 LSWLADTEELIANQkppSAEYKVVKAQIQ----EQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA--DREKITGQLESL 5425
Cdd:TIGR02168  830 ERRIAATERRLEDL---EEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLrsELEELSEELREL 906
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5426 ESRWTELLSKAAARQKQLEDI-LVLAK---QFHETAEPISDFLSVT-EKKLANSEPVGTQTAKIQQQIIRhkaLEEDIEN 5500
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLeLRLEGlevRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKR---LENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4547-5267 2.50e-11

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: 71.24  E-value: 2.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4547 EELNSRWERATEVTVARQRQLEESASHLACFQAAESQLRPWL----MEKELMMGVLGPLSIDPNMLNAQKQ-------QV 4615
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleEEIEELQKELYALANEISRLEQQKQilrerlaNL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4616 QFMLKEFEARRQQHEQLNEAAQGILTgpgdvslstsQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDL 4695
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4696 SEKVRAVGQRLSVQSAistqpeavkqqleETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKdELKKRLETVAlplQ 4775
Cdd:TIGR02168  385 RSKVAQLELQIASLNN-------------EIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---E 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4776 GLEDLAAdRINRLQAALASTqqfQQMFDELRTWLDDKQSQQAKncpISAKLERLQSQLQENEEFQKS-----LNQHSGSY 4850
Cdd:TIGR02168  448 ELEELQE-ELERLEEALEEL---REELEEAEQALDAAERELAQ---LQARLDSLERLQENLEGFSEGvkallKNQSGLSG 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4851 EVIVAegeSLLLSVPPGEEK-------RTLQNQLVELKNHWEE----LSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWI 4919
Cdd:TIGR02168  521 ILGVL---SELISVDEGYEAaieaalgGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4920 EDCKAKMSELRVTLDPVQ-LESSLLRSKAMLNEVEKRRSLLEILNSAADI------LINSSEADEDGIRDEKAGI---NQ 4989
Cdd:TIGR02168  598 EGFLGVAKDLVKFDPKLRkALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPGGVITGGSAKTNSSIlerRR 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4990 NMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEIFDALGSQAcsNKNLEKLRAQQE-VLQALEPQVDY 5068
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEqLEERIAQLSKE 755
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5069 LRNFTQGLVEDAPDGSDASQLLHQAEvaqQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQL-ADLDDELDGMGA 5147
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAE---AEIEELEAQIEQ----LKEELKALREALDELRAELTLLnEEAANLRERLES 828
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5148 IGRDTDSLQSQIEDVRlflNKIHVLKLDIEASEAECRHM--LEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLEL 5225
Cdd:TIGR02168  829 LERRIAATERRLEDLE---EQIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 2020023496 5226 TLGRVEDFYRKLKGLNDATTAAEEAEAlqwvvGTEVEIINQQ 5267
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLE-----GLEVRIDNLQ 942
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
44-173 3.26e-11

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: 63.51  E-value: 3.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   44 KKTFTKWVNKHL-MKVRKHINDLYEDLRDGHNLISLLEVLSGIKLEPaglktlrlvsmpswchtnneeqaeeddddvPRE 122
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK------------------------------INK 50
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2020023496  123 KGRMRFHRLQNVQIALDFLKQRQV-KLVNIRNDDIT-DGNPKLTLGLIWTIIL 173
Cdd:cd00014     51 KPKSPFKKRENINLFLNACKKLGLpELDLFEPEDLYeKGNLKKVLGTLWALAL 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4094-4835 3.27e-11

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: 70.86  E-value: 3.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4094 SLAERSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLEGKQVSSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 4173
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4174 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLAsgnQPDQDITHFF 4253
Cdd:TIGR02168  324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA---QLELQIASLN 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4254 QQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 4333
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4334 FQKWLKETEGSIPPTETSMSakELEKQIEHLKSLLDdwaskgtlveeinckgtslenlimeitapdSQGKTGSILPSVGS 4413
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQE--NLEGFSEGVKALLK------------------------------NQSGLSGILGVLSE 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4414 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGvlherqeSLQAILNRMEEVHKEANSVLQWLESKEE---VLKSMDAMS 4490
Cdd:TIGR02168  528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4491 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIQEE-----------LNSRW------ 4553
Cdd:TIGR02168  586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4554 ERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKE----LMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 4629
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRkeleELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4630 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQR 4705
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4706 LSV----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELS---VLIGEQY-------------------- 4758
Cdd:TIGR02168  826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELEselEALLNERasleealallrseleelsee 902
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4759 -------------LKDELKKRLETVALPLQGLEdlaaDRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAK 4825
Cdd:TIGR02168  903 lreleskrselrrELEELREKLAQLELRLEGLE----VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-----RR 973
                          810
                   ....*....|
gi 2020023496 4826 LERLQSQLQE 4835
Cdd:TIGR02168  974 LKRLENKIKE 983
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7146-7216 9.43e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 9.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 7146 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 7216
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4249-5069 1.30e-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: 68.93  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4249 ITHFFQQIQELNLEMEDQQENLDTLEHLVTELSScgfALDLCQHQ----DRVQNLRKDFTELQKTV-----KEREKDASS 4319
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLEDILNELER---QLKSLERQaekaERYKELKAELRELELALlvlrlEELREELEE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4320 CQEQLDEFRKLVRTFQKWLKETEGSIpptETSMSAK-ELEKQIEHLKSLLDDWASK-GTLVEEINCKGTSLENLIMEITA 4397
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKL---EELRLEVsELEEEIEELQKELYALANEiSRLEQQKQILRERLANLERQLEE 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4398 PDSQ-GKTGSILPSVGSSVGSVNgyhtcKDLTEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHKEANSVLQWL 4476
Cdd:TIGR02168  321 LEAQlEELESKLDELAEELAELE-----EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4477 ESKEEVLKSMDAMSSPTKTETVKAQAE----SNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAEnwKKIQEELnsr 4552
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEieelLKKLEEAELKELQAELEELEEELEELQEELERLEEAL--EELREEL--- 470
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4553 wERATEVTVARQRQLEESASHLACFQAAESQL-------RPWLMEKELMMGVLGPLS----IDP---------------- 4605
Cdd:TIGR02168  471 -EEAEQALDAAERELAQLQARLDSLERLQENLegfsegvKALLKNQSGLSGILGVLSelisVDEgyeaaieaalggrlqa 549
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4606 ---NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIdqAI 4682
Cdd:TIGR02168  550 vvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV--LV 627
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4683 VKS-TQYQELLQDLSEKVRAV---GQRLSVQSAISTQPEAVKQQLEETseiRSDLEQLDHEVKEAQTLCDELSV-LIGEQ 4757
Cdd:TIGR02168  628 VDDlDNALELAKKLRPGYRIVtldGDLVRPGGVITGGSAKTNSSILER---RREIEELEEKIEELEEKIAELEKaLAELR 704
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4758 YLKDELKKRLETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLQSQLQENE 4837
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE---LEERLEEAEEELAEAE 781
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4838 EFQKSLNQHSGSYEvivaegeslllsvppgEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVP 4917
Cdd:TIGR02168  782 AEIEELEAQIEQLK----------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4918 WIEDCKAKMSElrvtldpvqLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEE 4997
Cdd:TIGR02168  846 QIEELSEDIES---------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 4998 LQAKTGSLEEMTQRLREFQESFKNIEKKVEgAKHQLEIFDALgsqACSNKNLEKLRAQQEVLQALEPQVDYL 5069
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAE---ALENKIEDDEEEARRRLKRLENKIKEL 984
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7146-7208 1.60e-10

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 59.87  E-value: 1.60e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 7146 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 7208
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5559-5774 2.43e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.00  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5559 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 5638
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5639 KLDGIKTRYADITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELAtSGGQSPTGEQIPQFQQRQKELKKEVME 5718
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 5719 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 5774
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
5343-5444 3.68e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 3.68e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  5343 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 5422
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 2020023496  5423 ESLESRWTELLSKAAARQKQLE 5444
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4796-4899 3.79e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 3.79e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4796 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 4875
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 2020023496  4876 QLVELKNHWEELSKKTADRQSRLK 4899
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
40-171 4.72e-10

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: 60.24  E-value: 4.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   40 DRVQKKTFTKWVNKHLMKVR-KHINDLYEDLRDGHNLISLLEVLSGIKLEPAGLKtlrlvsmpswchtnneeqaeedddd 118
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDL------------------------- 56
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496  119 vpreKGRMRFHRLQNVQIALDFL-KQRQVKLVNIRNDDITDGNPKLTLGLIWTI 171
Cdd:cd21225     57 ----EPKNRIQMIQNLHLAMLFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
192-286 4.89e-10

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: 60.09  E-value: 4.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  192 KEKLLLWTQKVTAGytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 269
Cdd:cd21229      5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKReFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 2020023496  270 DVDVPSPDEKSVITYVS 286
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
SPEC smart00150
Spectrin repeats;
6218-6320 5.12e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 5.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6218 QYQDTLQAMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 6297
Cdd:smart00150    2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 2020023496  6298 LTELKHLWENLGEKIAHRQHKLE 6320
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
43-175 6.23e-10

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: 60.00  E-value: 6.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   43 QKKTFTKWVNKHLMK---VRKhINDLYEDLRDGHNLISLLEVLSGIKLEpaGLKTlrlvsmpswchtnneeqaeeddddV 119
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpgIRP-VQDLRRDLRDGVALAQLIEILAGEKLP--GIDW------------------------N 53
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496  120 PREKGRMRfhrlQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 175
Cdd:cd21213     54 PTTDAERK----ENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4587-4792 7.38e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 7.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4587 WLMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSlstSQVQKELQSINQKWVE 4666
Cdd:cd00176     15 WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA---EEIQERLEELNQRWEE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4667 LTDKLNSRSSQIDQAIVKSTQYQE---LLQDLSEKVRAVGQRLSVQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEA 4743
Cdd:cd00176     91 LRELAEERRQRLEEALDLQQFFRDaddLEQWLEEKEAALASEDLGKD-----LESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2020023496 4744 QTLCDELsVLIGEQYLKDELKKRLETVALPLQGLEDLAADRINRLQAAL 4792
Cdd:cd00176    166 NELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5120-6017 9.24e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 9.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5120 GIGQFHCRVREMFSQLADLDDELDgmgaigrdtdslqsQIEDVRLFLNKiHVLKLDIEASEAECRHMLEEEG-------- 5191
Cdd:TIGR02168  166 GISKYKERRKETERKLERTRENLD--------------RLEDILNELER-QLKSLERQAEKAERYKELKAELrelelall 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5192 TLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFyrklkglndattaaeeaealqwvvgteveiinqQLADF 5271
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------------------------------RLEVS 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5272 KMfqKEQVDPLQMKLQQVNGLgqgliqsagkdcdVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALlhcGKFQDALEPL 5351
Cdd:TIGR02168  278 EL--EEEIEELQKELYALANE-------------ISRLEQQKQILRERLANLERQLEELEAQLEELE---SKLDELAEEL 339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5352 LSWLADTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDrkatvdmlQAEGGRIAQSAELADREKITGQLESLESRwte 5431
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEE--------QLETLRSKVAQLELQIASLNNEIERLEAR--- 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5432 lLSKAAARQKQLEdilvlakqfhetaepisdflsvTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKI 5511
Cdd:TIGR02168  409 -LERLEDRRERLQ----------------------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5512 GQslssltspAEQGVLSEKIDSLQARYSEIQDRCcrkaALLDQALSNARLFGEDEVEVLNWLAEVEDKLSSVfvkdfkQD 5591
Cdd:TIGR02168  466 LR--------EELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVL------SE 527
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5592 VLHRQHADHLALNEEIVNRKKNV----DQAIKNGQALLKQTTGEEVLLIQekLDGIKtrYADITVTSSKALRTLEQARQL 5667
Cdd:TIGR02168  528 LISVDEGYEAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRVTFLP--LDSIK--GTEIQGNDREILKNIEGFLGV 603
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5668 ATKFQSTYEELTGWL---------------------------REV--EEELATSGGQSPTG------------------- 5699
Cdd:TIGR02168  604 AKDLVKFDPKLRKALsyllggvlvvddldnalelakklrpgyRIVtlDGDLVRPGGVITGGsaktnssilerrreieele 683
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5700 EQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLelvpwRAREGLDKLVSDANEQYKLVSDTIGQ---RVDEIDAAIQR 5776
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLR-----KELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTE 758
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5777 SQQYEQAADAELAWVAETKRKLMAlgpiRLEQDQTTAQlQVQKAFSIDIIRHKDSMDELFSHRSEIFGTcgEEQKTVLQE 5856
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA----EIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANL--RERLESLER 831
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5857 KTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpspaidHEQLRQQQEEMRQLRESIAE 5936
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEELSEELRE 905
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5937 HKPHIDKLLKigpQLKELNPEEGEMvEEKYQKAENMYAQIKEEVRQRA-LALDEAVsqstQFHDKIEPMLETLENLSSRL 6015
Cdd:TIGR02168  906 LESKRSELRR---ELEELREKLAQL-ELRLEGLEVRIDNLQERLSEEYsLTLEEAE----ALENKIEDDEEEARRRLKRL 977

                   ..
gi 2020023496 6016 RM 6017
Cdd:TIGR02168  978 EN 979
SPEC smart00150
Spectrin repeats;
6547-6648 1.23e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.88  E-value: 1.23e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6547 EFQNSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLIKNLL 6626
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 2020023496  6627 VSVQSRWEKVVQRSIERGRSLD 6648
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5670-5882 1.25e-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: 62.08  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5670 KFQSTYEELTGWLREVEEELA-TSGGQSPtgEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLELVPWRAREgLDKL 5748
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSsTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5749 VSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAElAWVAETKRKLMALGPIRLEQDqTTAQLQVQKAFSIDIIRH 5828
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5829 KDSMDELFSHRSEIFGTCGEEQKTVLQEKTESLIQQYEAISLLNSERYARLERA 5882
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4796-4900 1.63e-09

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 58.48  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4796 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 4875
Cdd:pfam00435    4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
                           90       100
                   ....*....|....*....|....*
gi 2020023496 4876 QLVELKNHWEELSKKTADRQSRLKD 4900
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
5888-5988 2.04e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.11  E-value: 2.04e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  5888 QFWETYEELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQ 5967
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  5968 KAENMYAQIKEEVRQRALALD 5988
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
43-174 2.11e-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: 58.67  E-value: 2.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   43 QKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSgiKLEPAGLktlrlvsmpSWCHTNneeqaeeddddVPRE 122
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDG---WVLLEVLD--KVSPGSV---------NWKHAN-----------KPPI 57
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2020023496  123 KgrMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILH 174
Cdd:cd21299     58 K--MPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2497-2535 4.01e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 4.01e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2497 LLTKQVVDGGIIHHISGMRLSVDNAFRHGLIGEDLAEKL 2535
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
4089-4788 7.08e-09

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: 63.06  E-value: 7.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4089 QSLSYSLAERSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLE-----GKQVSSLSSGVIQEALATNMKLKQDIARQKSS 4163
Cdd:TIGR00618  215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqqllKQLRARIEELRAQEAVLEETQERINRARKAAP 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4164 LEATREMVT--RFMETADSTTAAVLQGKLAEVSQRFEQLCLQQQEKES---SLKKLLPQAEMFEHLSGKLQQFMENKSRM 4238
Cdd:TIGR00618  295 LAAHIKAVTqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEqrrLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4239 LASGN---QPDQDITHFFQQIQELNLEMEDQQENLDTLEhlvtelsscgfALDLCQHQDRVQNLRKDFT-ELQKTVKERE 4314
Cdd:TIGR00618  375 HTLTQhihTLQQQKTTLTQKLQSLCKELDILQREQATID-----------TRTSAFRDLQGQLAHAKKQqELQQRYAELC 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4315 KDASSC--QEQLDEFRKLVRTFQKWlketegsipptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINCKGTSLENLI 4392
Cdd:TIGR00618  444 AAAITCtaQCEKLEKIHLQESAQSL-----------------KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4393 MEITAPDSQGKTGSILPSVGSS--VGSVNGYH---TCKDLTEIQCDMSDVNLKyeKLGGVLHERQESLQAILNRMEEVHK 4467
Cdd:TIGR00618  507 CGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAqleTSEEDVYHQLTSERKQRA--SLKEQMQEIQQSFSILTQCDNRSKE 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4468 EANSVLQWLES----KEEVLKSMDAMSSPTKTETVKAQAESNKAFLAELEQN-SPKIQKVKEALAGLLVTYPNSQEAENW 4542
Cdd:TIGR00618  585 DIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQERVREHA 664
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4543 ---KKIQEELNSRWERATEVTVARQRQ-------LEESASHLACFQAAESQLRPWLMEKELMMGVLGplsidpNMLNAQK 4612
Cdd:TIGR00618  665 lsiRVLPKELLASRQLALQKMQSEKEQltywkemLAQCQTLLRELETHIEEYDREFNEIENASSSLG------SDLAARE 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4613 QQVQFMLKEFEARR--QQHEQLNEAAQGILTGPGDVSLST--SQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQY 4688
Cdd:TIGR00618  739 DALNQSLKELMHQArtVLKARTEAHFNNNEEVTAALQTGAelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4689 QELLQDLSEKVRA-VGQRLSVQSAISTQpeaVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKDELKKRL 4767
Cdd:TIGR00618  819 LNLQCETLVQEEEqFLSRLEEKSATLGE---ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIK 895
                          730       740
                   ....*....|....*....|.
gi 2020023496 4768 ETVALPLQGLEDLAADRINRL 4788
Cdd:TIGR00618  896 FLHEITLYANVRLANQSEGRF 916
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
61-172 9.27e-09

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: 56.83  E-value: 9.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   61 HINDLYEDLRDGHNLISLLEVLSGiklEPAGLKTLRLVSmpswchtnneeqaeeddddvpreKGRMRfhRLQNVQIALDF 140
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVPA-----------------------ISRLQ--KLHNVEVALKA 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2020023496  141 LKQRQV----KLVNIRNDDITDGNPKLTLGLIWTII 172
Cdd:cd21223     77 LKEAGVlrggDGGGITAKDIVDGHREKTLALLWRII 112
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
190-294 1.07e-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: 56.62  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  190 SAKEKLLLWTQ-KVTAgytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DME----RVQIQSNRENLEQAfevAERLGVT 263
Cdd:cd21314     11 TPKQRLLGWIQnKVPQ----LPITNFNRDWQDGKALGALVDNCAPGLCpDWEswdpNQPVQNAREAMQQA---DDWLGVP 83
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2020023496  264 RLLDAEDVDVPSPDEKSVITYVSSiydaFPK 294
Cdd:cd21314     84 QVIAPEEIVDPNVDEHSVMTYLSQ----FPK 110
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4904-5108 1.11e-08

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.38  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4904 KAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDE 4983
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4984 KAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKnIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALE 5063
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2020023496 5064 PQVDYLRNFTQGLVEDAPDGSDAsQLLHQAEVAQQEFLEVKQRVN 5108
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAE 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3686-4369 1.63e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3686 LSPRELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALldwvtsvgssgGQLL 3765
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-----------ANEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3766 TNLPGMEQLSGASLekgaldttdgymgvnqapEKLDKQCEMMKARHQELLSQQQNFILATQSAQafldqhghnltpEEQQ 3845
Cdd:TIGR02168  298 SRLEQQKQILRERL------------------ANLERQLEELEAQLEELESKLDELAEELAELE------------EKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3846 MLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLERSEKELENMHkggsspETLPSLLKRQGSFSE 3925
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE------ARLERLEDRRERLQQ 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3926 DVISHKGDL---RFVTISGQKV-LDMENSFKEGKEPSEIGNL--VKDKLKDATERYTALHSKCTRLGSHLNMLLGQYHQF 3999
Cdd:TIGR02168  422 EIEELLKKLeeaELKELQAELEeLEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4000 QNSADSLQAWMQACE--ANVEKLLSDTVASDPG---------------VLQEQLATTKQLQEELAEHqvpveKLQKVArd 4062
Cdd:TIGR02168  502 EGFSEGVKALLKNQSglSGILGVLSELISVDEGyeaaieaalggrlqaVVVENLNAAKKAIAFLKQN-----ELGRVT-- 574
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4063 IMEI----EGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSqSVQESLESLLQSIGEVEQN-----LEGK 4133
Cdd:TIGR02168  575 FLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALELAKKLRPGyrivtLDGD 653
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4134 QVSslSSGVI-QEALATNMKLkqdIARQKSSLEATREMvTRFMETADSTTAAV--LQGKLAEVSQRFEQLCLQQQEKESS 4210
Cdd:TIGR02168  654 LVR--PGGVItGGSAKTNSSI---LERRREIEELEEKI-EELEEKIAELEKALaeLRKELEELEEELEQLRKELEELSRQ 727
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4211 LKKLLPQAEMFEHLSGKLQQFMENKSRMLASGNQP----DQDITHFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGFA 4286
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4287 LdlcqhQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMSakELEKQIEHLKS 4366
Cdd:TIGR02168  808 L-----RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE--ELESELEALLN 880

                   ...
gi 2020023496 4367 LLD 4369
Cdd:TIGR02168  881 ERA 883
EF-hand_7 pfam13499
EF-hand domain pair;
7144-7207 1.92e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 7144 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 7207
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
185-294 3.30e-08

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: 55.10  E-value: 3.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  185 ESGDMSAKEKLLLWTQKVTAgYTGIkcTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGV 262
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIP-YLPI--TNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDwLGV 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2020023496  263 TRLLDAEDVDVPSPDEKSVITYVSSiydaFPK 294
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQ----FPK 107
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
187-294 4.10e-08

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: 55.17  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  187 GDMSAKEKLLLWTQ-KVTagytGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVT 263
Cdd:cd21315     13 KGPTPKQRLLGWIQsKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDwLDVP 88
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2020023496  264 RLLDAEDVDVPSPDEKSVITYVSsiydAFPK 294
Cdd:cd21315     89 QLIKPEEMVNPKVDELSMMTYLS----QFPN 115
SPEC smart00150
Spectrin repeats;
6875-6975 4.93e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.26  E-value: 4.93e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6875 FRDTVHMLLEWLSEAEQTLRFRGaLPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWIT 6954
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  6955 IIRARFEEVLTWAKQHQQRLE 6975
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4460-4569 4.96e-08

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 4.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4460 NRMEEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 4539
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 2020023496 4540 ENWKKiQEELNSRWERATEVTVARQRQLEE 4569
Cdd:pfam00435   77 EIQER-LEELNERWEQLLELAAERKQKLEE 105
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7149-7207 5.47e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 5.47e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 7149 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 7207
Cdd:COG5126     37 TLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL 95
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6766-6867 6.39e-08

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 6.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6766 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 6845
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 2020023496 6846 ELSTRWDTVCKLSVSKQSRLEQ 6867
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3486-3722 6.58e-08

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.07  E-value: 6.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3486 QLEGRLQDLRAWVGNKNLILNSKGSNSeiDVDSLNLCLQQYEDLKQPMAERKAQLDALAFDIQFFISEHAQDLSPQQNRq 3565
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3566 mlrlLNELQRSFQDILEQTAAQVDALQGHLQQMEQealvktlqkqqntcHQQLEDLCSWVGQAERALAGHQgrtTQQDLS 3645
Cdd:cd00176     81 ----LEELNQRWEELRELAEERRQRLEEALDLQQF--------------FRDADDLEQWLEEKEAALASED---LGKDLE 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020023496 3646 ALQKNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENQtklsPRELTALREKLHQAKEQYEALQEETRVAQKELEEA 3722
Cdd:cd00176    140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4108-4315 7.93e-08

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 56.69  E-value: 7.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4108 QSQSVQESLESLLQSIGEVEQNLEGKQVSSLSSGViQEALATNMKLKQDIARQKSSLEATREMVTRFMEtADSTTAAVLQ 4187
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4188 GKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSgKLQQFMENKSRMLASGNQPD--QDITHFFQQIQELNLEMED 4265
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4266 QQENLDTLEHLVTELSSCGFALDLCQHQDRVQNLRKDFTELQKTVKEREK 4315
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC smart00150
Spectrin repeats;
6108-6210 8.67e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 8.67e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6108 EKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVRKS 6187
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 2020023496  6188 IDEMNNAWENLNKTWKERLEKLE 6210
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1574-1612 1.05e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 51.17  E-value: 1.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1574 LLESQVIMSGLIAPETGENLSLEEGIARNLINPQMYQQL 1612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
6436-6539 1.13e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 1.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6436 QGFHSEIEDFLLELTRMESQLSaSKPTGGLPETAREQLDTHMELYSQLKAKEETYNQLLDKGRLMLlsRDDSGSGSKTEQ 6515
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 2020023496  6516 SVALLEQKWHVVSSKMEERKSKLE 6539
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1764-1800 1.48e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 50.94  E-value: 1.48e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2020023496  1764 RLLEAQLFAGGIVDPRTGHRLTVEEAVRHNLIDQDMA 1800
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2683-2721 1.62e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 50.79  E-value: 1.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2683 VLEAQANTGGIIDTATGKRLTLASALEEKLVDENMVRII 2721
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5343-5445 2.86e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5343 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSaELADREKITGQL 5422
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 2020023496 5423 ESLESRWTELLSKAAARQKQLED 5445
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
3995-4103 2.89e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3995 QYHQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 4074
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKE---ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
                           90       100
                   ....*....|....*....|....*....
gi 2020023496 4075 RHVQETTDSILSHFQSLSYSLAERSSLLQ 4103
Cdd:pfam00435   76 EEIQERLEELNERWEQLLELAAERKQKLE 104
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
4609-5033 3.30e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.82  E-value: 3.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4609 NAQKQQVQFMLKEFEARRQ-QHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELT-DKLNSRSSQidqaivksT 4686
Cdd:pfam15921  425 NMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTaKKMTLESSE--------R 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4687 QYQELLQDLSEKVRAVGqrlSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHevkeAQTLCDELSVLIGEqylKDelkKR 4766
Cdd:pfam15921  497 TVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALKLQMAE---KD---KV 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4767 LETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNcpiSAKLERLQSQLQENEEFQKSLnqh 4846
Cdd:pfam15921  564 IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKK---DAKIRELEARVSDLELEKVKL--- 637
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4847 sgsyeviVAEGESLLLSVPPGEEKRtlqNQLV-ELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAK 4925
Cdd:pfam15921  638 -------VNAGSERLRAVKDIKQER---DQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4926 MSELRVTLDPVQLES--SLLRSKAMLNEVEKRRSLLEILNSAADIL---INSSEADEDGIRDEKAGINQNMDAVTEELQA 5000
Cdd:pfam15921  708 LEQTRNTLKSMEGSDghAMKVAMGMQKQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2020023496 5001 KTGSLEEMTQRLREFQESFKNIEKKVEGAKHQL 5033
Cdd:pfam15921  788 MAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
SPEC smart00150
Spectrin repeats;
4463-4568 3.70e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 3.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4463 EEVHKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 4542
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 2020023496  4543 KKIQEELNSRWERATEVTVARQRQLE 4568
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
44-172 3.86e-07

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: 52.19  E-value: 3.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   44 KKTFTKWVNKHLMKVR--KHI-------NDLYEDLRDGHNLISLLEvlsgiKLEPaGLKTLRLVSMpswCHTNNEeqaee 114
Cdd:cd21217      3 KEAFVEHINSLLADDPdlKHLlpidpdgDDLFEALRDGVLLCKLIN-----KIVP-GTIDERKLNK---KKPKNI----- 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496  115 ddddvprekgrmrFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTII 172
Cdd:cd21217     69 -------------FEATENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4186-5026 3.98e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 3.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4186 LQGKLAEVSQRFEQLCLQQQEKES--SLKKLLPQAEMFEHLsGKLQQFMENKSRMLASGNQPDQDITHFFQQIQELNLEM 4263
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYELL-KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4264 EDQQENLDTLEHLVTELSScgfaldlcqhqdrvqnlrKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEG 4343
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGE------------------EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4344 SIPPTETSMsaKELEKQIEHLKSLLDDWAskgtlvEEINCKGTSLENLIMEITAPDSQGKTgsilpsvgssvgsvngyhT 4423
Cdd:TIGR02169  330 EIDKLLAEI--EELEREIEEERKRRDKLT------EEYAELKEELEDLRAELEEVDKEFAE------------------T 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4424 CKDLTEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHKEANSVLQWLESKEEVLKSMDA--MSSPTKTETVKAQ 4501
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeiKKQEWKLEQLAAD 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4502 AESNKAFL----AELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIQEELNSRWERATEVTVARQRQLEEsASHLACF 4577
Cdd:TIGR02169  464 LSKYEQELydlkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGE-RYATAIE 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4578 QAAESQLRPWLMEKELMmgvlgplsidpnmlnaQKQQVQFmLKEFEARRQQHEQLNEAAQ-----GILTGPGDVSLSTSQ 4652
Cdd:TIGR02169  543 VAAGNRLNNVVVEDDAV----------------AKEAIEL-LKRRKAGRATFLPLNKMRDerrdlSILSEDGVIGFAVDL 605
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4653 VQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRA-VGQRLSVQSAIS---TQPEAVKQQLEETSE 4728
Cdd:TIGR02169  606 VEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAmTGGSRAPRGGILfsrSEPAELQRLRERLEG 685
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4729 IRSDLEQLDHEVKEAQTLCDELSVLIgeqylkDELKKRLETVALPLQGLEDLAA---DRINRLQAALASTQQ----FQQM 4801
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQEL------SDASRKIGEIEKEIEQLEQEEEklkERLEELEEDLSSLEQeienVKSE 759
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4802 FDELRTWLDDKQSQQAKNCPISAKLER--LQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPG-----EEKRTLQ 4874
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyleKEIQELQ 839
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4875 NQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ-----LESSLLRSKAML 4949
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeLEAQIEKKRKRL 919
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4950 NEVEKRRSLLEILNS------AADILINSSEADEDGIRDEKAGINQ--------NMDAVTE---------ELQAKTGSLE 5006
Cdd:TIGR02169  920 SELKAKLEALEEELSeiedpkGEDEEIPEEELSLEDVQAELQRVEEeiralepvNMLAIQEyeevlkrldELKEKRAKLE 999
                          890       900
                   ....*....|....*....|
gi 2020023496 5007 EMTQRLREFQESFKNIEKKV 5026
Cdd:TIGR02169 1000 EERKAILERIEEYEKKKREV 1019
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3551-3901 4.03e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3551 ISEHAQDLSPQQNRQMLRLLNELQRSFQDI--LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQA 3628
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELkeAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3629 ERALAGHQGRTTQQDLS----ALQKNQSDLKDLQDDIQNRATSFATVVKDIEgfMEENQTKLspreltALREKLHQAKEQ 3704
Cdd:COG4717    129 PLYQELEALEAELAELPerleELEERLEELRELEEELEELEAELAELQEELE--ELLEQLSL------ATEEELQDLAEE 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3705 YEALQEETRVAQKELEEAVT--SALQQETEKSKAAKELAENKKKIDALLDWVTSVgssGGQLLTNLPGMEQLSGASLEKG 3782
Cdd:COG4717    201 LEELQQRLAELEEELEEAQEelEELEEELEQLENELEAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTIAG 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3783 ALDTTDGYMGVnqAPEKLDKQCEMMKARHQELLSQQQNFILATQSAQAFLDQHG--HNLTPEEQQMLQQKLGELKEQYSt 3860
Cdd:COG4717    278 VLFLVLGLLAL--LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLR- 354
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2020023496 3861 SLAQSEAELkQVQTLQDELQKFLQ-----DHKEFESWLERSEKELE 3901
Cdd:COG4717    355 EAEELEEEL-QLEELEQEIAALLAeagveDEEELRAALEQAEEYQE 399
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6656-6759 6.99e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.17  E-value: 6.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6656 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDSQKLDNF 6735
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE--GHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 2020023496 6736 LGEVRDKWDTVCGKSVERQHKLEE 6759
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
7149-7208 7.57e-07

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 49.91  E-value: 7.57e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020023496 7149 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLemtavADIF---DRDGDGYIDYYEFVAALH 7208
Cdd:cd00052      3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL-----AQIWdlaDTDKDGKLDKEEFAIAMH 60
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
38-177 1.04e-06

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: 51.54  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSGIKLePAglktlrlvsmpSWCHTNNEeqaeeddd 117
Cdd:cd21331     18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDA---LVILQLYEKIKV-PV-----------DWNKVNKP-------- 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496  118 dvPREKGRMRFHRLQNVQIALDFLKQR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 177
Cdd:cd21331     73 --PYPKLGANMKKLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6543-6649 1.09e-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: 50.78  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6543 NLATEFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLI 6622
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 2020023496 6623 KNLLVSVQSRWEKVVQRSIERGRSLDD 6649
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
3534-3752 1.29e-06

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: 54.77  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3534 AERKAQLDALAFDIQffisehaqdlspqQNRQMLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQ-----EALVKTLQ 3608
Cdd:COG4942     23 AEAEAELEQLQQEIA-------------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaalEAELAELE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3609 KQQNTCHQQLEDLCSWVGQAERALAghqgRTTQQDLSALQKNQSDLKDLqddiQNRATSFATVVKDIEGFMEENQTKLsp 3688
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALY----RLGRQPPLALLLSPEDFLDA----VRRLQYLKYLAPARREQAEELRADL-- 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 3689 RELTALREKLHQAKEQYEALQEETRVAQKELEEA-------VTSALQQETEKSKAAKELAENKKKIDALLD 3752
Cdd:COG4942    160 AELAALRAELEAERAELEALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIA 230
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
4448-5107 1.56e-06

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: 55.36  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4448 LHERQESLQAILNRMEEVHKEANSVLQWLESKEEVLKSMDAMSSPTKteTVKAQAESNKAFLAELEQNSPKI----QKVK 4523
Cdd:TIGR00618  217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrarKAAP 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4524 EALAGLLVTYPNSQEAENWKKIQEELNSRW-ERATEVTVARQRQ-LEESASHLACFQAAESQLRPWLMEKELMMGVLGPL 4601
Cdd:TIGR00618  295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4602 SIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAqgiltgpgdvslstSQVQKELQSINqkwVELTDKLNSRSSQidqa 4681
Cdd:TIGR00618  375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ--------------ATIDTRTSAFR---DLQGQLAHAKKQQ---- 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4682 iVKSTQYQELLQDLSEKVravgqrlsVQSAISTQPEAVK--QQLEETSEIRSDLEQLDHEVKEAQTLcdELSVLIGEQYL 4759
Cdd:TIGR00618  434 -ELQQRYAELCAAAITCT--------AQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHLQETRKKAV--VLARLLELQEE 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4760 KDELKKRLETVALPLQGLEDLAADRiNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLQsqlQENEEF 4839
Cdd:TIGR00618  503 PCPLCGSCIHPNPARQDIDNPGPLT-RRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS---LKEQMQEIQ---QSFSIL 575
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4840 QKSLNQHSGSYEVIVAEGESLLLSVPpgEEKRTLQNQLVELKNHWEELSKKTADRQSRLKD--CMQKAQKYQWHVEDLVP 4917
Cdd:TIGR00618  576 TQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqqCSQELALKLTALHALQL 653
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4918 WIEDCKAKMSELRVTLDPVQ-LESSLLRSKAMLNEVEKRRSLLEILNSaADILINSSEADEDGIRDEKAGINQNMDAVTE 4996
Cdd:TIGR00618  654 TLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQ-CQTLLRELETHIEEYDREFNEIENASSSLGS 732
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4997 ELQAKTGSLEEMTQRLR-EFQESFKNIEKKVEGAKHQLEIFDALGSQacsnknLEKLRAQQEVLQ-ALEPQVDYLRNFTQ 5074
Cdd:TIGR00618  733 DLAAREDALNQSLKELMhQARTVLKARTEAHFNNNEEVTAALQTGAE------LSHLAAEIQFFNrLREEDTHLLKTLEA 806
                          650       660       670
                   ....*....|....*....|....*....|...
gi 2020023496 5075 GLVEDAPDGSDAsqLLHQAEVAQQEFLEVKQRV 5107
Cdd:TIGR00618  807 EIGQEIPSDEDI--LNLQCETLVQEEEQFLSRL 837
SPEC smart00150
Spectrin repeats;
6988-7112 1.72e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 1.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  6988 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 7066
Cdd:smart00150    7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 2020023496  7067 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 7112
Cdd:smart00150   78 ----------------------RLEELNERWEELKELAEERRQKLE 101
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
38-178 1.99e-06

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: 50.37  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   38 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEvlsgiklepaglktlrLVSMP-SWCHTNNEEqaeedd 116
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYE----------------MTRVPvDWGHVNKPP------ 57
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020023496  117 ddVPREKGRMRfhRLQNVQIALDFLKQR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 178
Cdd:cd21329     58 --YPALGGNMK--KIENCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5371-5934 2.50e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5371 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLESLESRWTELLSKAAARQKQLEDIL-VL 5449
Cdd:COG1196    214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5450 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 5523
Cdd:COG1196    291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5524 QGVLSEKIDSLQARYSEIQDRCCRKAALLDQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQHADHLAL 5603
Cdd:COG1196    371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5604 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYADIT---------VTSSKALRTLEQARQLATKFQst 5674
Cdd:COG1196    451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5675 yeELTGWLREVEEELATSGG---QSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 5746
Cdd:COG1196    528 --VLIGVEAAYEAALEAALAaalQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5747 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 5826
Cdd:COG1196    606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5827 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 5906
Cdd:COG1196    685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
                          570       580
                   ....*....|....*....|....*...
gi 2020023496 5907 IAQLPSPAIDHEQLRQQQEEMRQLRESI 5934
Cdd:COG1196    752 ALEELPEPPDLEELERELERLEREIEAL 779
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5123-5338 3.23e-06

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5123 QFHCRVREMFSQLADLDDELDGMGaIGRDTDSLQSQIEDVRLFLNKIHVLKLDIEASEAECRHMLEEeGTLDLLGLKREL 5202
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5203 EALNKQCGKLTERGKARQEQLELTLGRVEdFYRKLKGLNDATTAAEEAEALQwVVGTEVEIINQQLADFKMFQKEqVDPL 5282
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEE-LEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 5283 QMKLQQVNGLGQGLIQSAGKDcDVQGLEHDMEEINARWNTLNKKVAQRIAQLQEAL 5338
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
3524-4200 3.67e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3524 QQYEDLKQPMAERKAQLDALAfDIQFFISEHAQDLSPQQNRQMLRLlnELQRSF-QDILEQTAAQVDAL-------QGHL 3595
Cdd:pfam15921  110 QSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQLQNTVHEL--EAAKCLkEDMLEDSNTQIEQLrkmmlshEGVL 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3596 QQME------QEALVKTLQKQQNTCHQQLEDLCSWVGQAERALaghqgrttQQDLSALQKN----QSDLKDLQDDIQNRA 3665
Cdd:pfam15921  187 QEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILREL--------DTEISYLKGRifpvEDQLEALKSESQNKI 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3666 TSFATVVKD-IEGFMEENQTklsprELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQ----ETEKSKAAKEL 3740
Cdd:pfam15921  259 ELLLQQHQDrIEQLISEHEV-----EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQlsdlESTVSQLRSEL 333
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3741 AENKK----KIDALLDWVTSVGSSGGQLLTNLPGMEQlsgaslEKGALDttdgymgvnqapEKLDKQCEMMKARHQEL-L 3815
Cdd:pfam15921  334 REAKRmyedKIEELEKQLVLANSELTEARTERDQFSQ------ESGNLD------------DQLQKLLADLHKREKELsL 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3816 SQQQNFILATQ-SAQAFLDQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLE 3894
Cdd:pfam15921  396 EKEQNKRLWDRdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE 475
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3895 RSEKELENMHKGGSSPETlpsllkrqgsfSEDVIShkgdlrfvtisgqkvlDMENSFKEgkepseignlvKDKLKDATer 3974
Cdd:pfam15921  476 MLRKVVEELTAKKMTLES-----------SERTVS----------------DLTASLQE-----------KERAIEAT-- 515
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3975 ytalHSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEA-NVEKLLSDTVASdpgVLQEQLATTKQL--QEELAEHQV 4051
Cdd:pfam15921  516 ----NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDKVIE---ILRQQIENMTQLvgQHGRTAGAM 588
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4052 PVEKLQ---------------KVARD-----IMEIEGEPAPDHRHVQETTDSILSHFQSLSYSLAERSSLLQKAiaqsQS 4111
Cdd:pfam15921  589 QVEKAQlekeindrrlelqefKILKDkkdakIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV----KT 664
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4112 VQESLESLLQSIGEVEQNLEGKQvsslssgviQEALATNMKLKQDIARQKSSLEATREMVtRFMETADSTTAAVLQGKLA 4191
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFRNKS---------EEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHAMKVAMGMQK 734

                   ....*....
gi 2020023496 4192 EVSQRFEQL 4200
Cdd:pfam15921  735 QITAKRGQI 743
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3408-3750 4.07e-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: 54.29  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3408 ERELKDLTtlvsQELECVNQIIISQPQEvpaqlLKALEKDAKNLQKSLSSVSDTWNsRLLHFQNAVEIEKTKVLNQHTQL 3487
Cdd:TIGR02168  676 RREIEELE----EKIEELEEKIAELEKA-----LAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3488 EGRLQDLRAWVGNKNLILNSKGSNSEIDVDSLNLCLQQYEDLKQPMAERKAQLDALAfdiqffisehaQDLSPQQNRqmL 3567
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----------EALDELRAE--L 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3568 RLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTchQQLEDLCSWVGQAERALAGHQGRTTQQDLsAL 3647
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEE-AL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3648 QKNQSDLKDLQDDIQNratsfatvvkdiegfMEENQTKLSpRELTALREKLHQAKEQYEALQEE--------TRVAQKEL 3719
Cdd:TIGR02168  890 ALLRSELEELSEELRE---------------LESKRSELR-RELEELREKLAQLELRLEGLEVRidnlqerlSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2020023496 3720 EEAVTSALQQETEKSKAAKELAENKKKIDAL 3750
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4448-5161 4.47e-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: 53.91  E-value: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4448 LHERQESLQAILNRMEEVHKEANSVLQWLESKEEVLKSMDamsSPTKTETVKAQAESN--KAFLAELEQNspkIQKVKEA 4525
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV---SELEEEIEELQKELYalANEISRLEQQ---KQILRER 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4526 LAGLLVTYP--NSQEAENWKKI---QEELNSRWERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKELMMGVLGP 4600
Cdd:TIGR02168  311 LANLERQLEelEAQLEELESKLdelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4601 LSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILtgpgdVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQ 4680
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQAELEELEEELEELQEELERLEEALEE 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4681 AIVKSTQYQELLQDLSEKVRAVGQRL----SVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGE 4756
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQARLdsleRLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGG 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4757 --QYLkdeLKKRLETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLQS--- 4831
Cdd:TIGR02168  546 rlQAV---VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyll 622
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4832 -------QLQENEEFQKSLNQHsgsYEVIVAEGESLLL--SVPPGEEKRT--LQNQLVELKNHWEELSK---KTADRQSR 4897
Cdd:TIGR02168  623 ggvlvvdDLDNALELAKKLRPG---YRIVTLDGDLVRPggVITGGSAKTNssILERRREIEELEEKIEEleeKIAELEKA 699
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4898 LKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELR------------VTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSA 4965
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRkdlarleaeveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4966 ADILINSSEADEDGIRDEKAGINQNMDAVTEELQA-------KTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEifDA 5038
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SL 857
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5039 LGSQACSNKNLEKLRAQQEVLQALEPQVDylrnftQGLVEDAPDGSDASQLLHQAEVAQQEFLEVKQRVNSGCVMMENKL 5118
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLE------EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....
gi 2020023496 5119 EGIGQfhcRVREMFSQLADL-DDELDGMGAIGRDTDSLQSQIED 5161
Cdd:TIGR02168  932 EGLEV---RIDNLQERLSEEySLTLEEAEALENKIEDDEEEARR 972
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5011-5224 5.53e-06

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 51.29  E-value: 5.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5011 RLREFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDgsDASQLL 5090
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5091 HQAEVAQQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQLADLDDELDGMGA--IGRDTDSLQSQIEDVRLFLNK 5168
Cdd:cd00176     79 ERLEELNQRWEELRELAEE----RRQRLEEALDLQQFFRDADDLEQWLEEKEAALASedLGKDLESVEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 5169 IHVLKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLE 5224
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
3578-3752 5.83e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 5.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3578 QDILEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTQQdLSALQKNQSDLKDL 3657
Cdd:COG3883     29 QAELEAAQAELDALQAELEELNEE--YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3658 qDDIQNrATSFATVVKDIEG---FMEENQTKLspRELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKS 3734
Cdd:COG3883    106 -DVLLG-SESFSDFLDRLSAlskIADADADLL--EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
                          170
                   ....*....|....*...
gi 2020023496 3735 KAAKELAENKKKIDALLD 3752
Cdd:COG3883    182 ALLAQLSAEEAAAEAQLA 199
SPEC smart00150
Spectrin repeats;
5452-5551 5.94e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 5.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  5452 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLSEKI 5531
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEERL 79
                            90       100
                    ....*....|....*....|.
gi 2020023496  5532 DSLQARYSEIQDRC-CRKAAL 5551
Cdd:smart00150   80 EELNERWEELKELAeERRQKL 100
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
188-290 6.25e-06

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: 48.83  E-value: 6.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  188 DMSAKEKLLLWTQK--VTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVD----MERVQIQSNRENLEQAFEVAERLG 261
Cdd:cd21218      8 YLPPEEILLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLG 87
                           90       100
                   ....*....|....*....|....*....
gi 2020023496  262 VTRLLDAEDVdVpSPDEKSVITYVSSIYD 290
Cdd:cd21218     88 CKYFLTPEDI-V-SGNPRLNLAFVATLFN 114
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1803-1841 7.62e-06

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.17  E-value: 7.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1803 ILIRQLQTGGIIDTVTGQRLTIDEAVSNDLVAAKIALVI 1841
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
3551-4269 8.90e-06

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: 53.05  E-value: 8.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3551 ISEHAQDLSpQQNRQMLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTCHQQLEDLCSWVGQAER 3630
Cdd:TIGR00618  295 LAAHIKAVT-QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3631 ALAGHQG-RTTQQDLSALQKNQSDLKDLQDDIQNRATSFATV-----VKDIEGFMEENQTKLSPRELTALR---EKLHQA 3701
Cdd:TIGR00618  374 QHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsafrDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQC 453
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3702 KEQYEALQEETRVAQKELEEA---VTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLLTNLPGMEQLSGAS 3778
Cdd:TIGR00618  454 EKLEKIHLQESAQSLKEREQQlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3779 LekgaldttDGYMGVNQAPEKLDKQCEMMKARHQELLSQ----QQNFILATQSAQAFLDQHghNLTPEEQQMLQQKLGEL 3854
Cdd:TIGR00618  534 E--------QTYAQLETSEEDVYHQLTSERKQRASLKEQmqeiQQSFSILTQCDNRSKEDI--PNLQNITVRLQDLTEKL 603
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3855 KEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFEswlersEKELENMHKGGSSpETLPSLLKRQGSFSEDVIshkgdl 3934
Cdd:TIGR00618  604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ------ELALKLTALHALQ-LTLTQERVREHALSIRVL------ 670
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3935 rfvtisgQKVLDMENSFKEGKEPSEIGNLVKDKlKDATERYTALHSKCTRLGShlnmLLGQYHQFQNSADSLQAWMQACE 4014
Cdd:TIGR00618  671 -------PKELLASRQLALQKMQSEKEQLTYWK-EMLAQCQTLLRELETHIEE----YDREFNEIENASSSLGSDLAARE 738
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4015 ANVEKLLsdtvasdpGVLQEQLATtkQLQEELAEHQvpveklQKVARDIMEIegepapdhrhvqettdsilshfqslsYS 4094
Cdd:TIGR00618  739 DALNQSL--------KELMHQART--VLKARTEAHF------NNNEEVTAAL--------------------------QT 776
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4095 LAERSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLEGKQvsslssgviQEALATNMKLKQDIARQKSSLEatremvtrf 4174
Cdd:TIGR00618  777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE---------DILNLQCETLVQEEEQFLSRLE--------- 838
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4175 METADSTTAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLlpqaemfEHLSGKLQQFMENKSRMLASGNQPDQDITHFFQ 4254
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL-------NGINQIKIQFDGDALIKFLHEITLYANVRLANQ 911
                          730
                   ....*....|....*
gi 2020023496 4255 QIQELNLEMEDQQEN 4269
Cdd:TIGR00618  912 SEGRFHGRYADSHVN 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3556-3879 1.18e-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: 52.75  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3556 QDLSPQQNRQMLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGH 3635
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE--LEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3636 QGRTTQQDLSALQKNQ------SDLKDLQDDIQNRATSFATVVKDIEGFMEENQT------KLSpRELTALREKLHQAKE 3703
Cdd:TIGR02168  746 EERIAQLSKELTELEAeieeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdELR-AELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3704 QYEALQEETRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLltnlpgMEQLSGASLEKGA 3783
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3784 LDTTdgymgVNQAPEKLDKqcemMKARHQELLSQQQNFILATQSAQAFLDQHGHNLTpEEQQMLQQKLGELKEQYSTSLA 3863
Cdd:TIGR02168  899 LSEE-----LRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAEALENKIEDDEE 968
                          330
                   ....*....|....*.
gi 2020023496 3864 QSEAELKQVQTLQDEL 3879
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
SPEC smart00150
Spectrin repeats;
581-675 1.37e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.32  E-value: 1.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   581 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYA---ETLGKLE 657
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEeieERLEELN 83
                            90
                    ....*....|....*...
gi 2020023496   658 TQYCKLKETSSFRMRHLQ 675
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
3997-4103 1.45e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.32  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  3997 HQFQNSADSLQAWMQACEanvEKLLSDTVASDPGVLQEQLATTKQLQEELAEHQVPVEKLQKVARDIMEIEGEPAPDhrh 4076
Cdd:smart00150    1 QQFLRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--- 74
                            90       100
                    ....*....|....*....|....*..
gi 2020023496  4077 VQETTDSILSHFQSLSYSLAERSSLLQ 4103
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
678-770 1.70e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   678 HKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYSA 757
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2020023496   758 AVQSQLQWMKQLC 770
Cdd:smart00150   81 ELNERWEELKELA 93
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6218-6320 2.15e-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: 46.93  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6218 QYQDTLQAMFDWLDNTVIKLcTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 6297
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
                           90       100
                   ....*....|....*....|...
gi 2020023496 6298 LTELKHLWENLGEKIAHRQHKLE 6320
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4217-4459 2.75e-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: 48.98  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4217 QAEMFEHLSGKLQQFMENKSRMLASGNQPD--QDITHFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGfALDLCQHQD 4294
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDdlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4295 RVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKlVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASK 4374
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4375 GTLVEEINCKGTSLENLimeitapdsqgktgsilpsvgssvgsvngyHTCKDLTEIQCDMSDVNLKYEKLGGVLHERQES 4454
Cdd:cd00176    159 EPRLKSLNELAEELLEE------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKK 208

                   ....*
gi 2020023496 4455 LQAIL 4459
Cdd:cd00176    209 LEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6882-6975 3.23e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6882 LLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWITIIRARFE 6961
Cdd:pfam00435   13 LESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWE 90
                           90
                   ....*....|....
gi 2020023496 6962 EVLTWAKQHQQRLE 6975
Cdd:pfam00435   91 QLLELAAERKQKLE 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5848-6492 3.36e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5848 EEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpspaidHEQLRQQQEEM 5927
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL------EQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5928 RQLRESIAEHKPHIDKLLK-----------IGPQLKELNPE------EGEMVEEKYQKAENMYAQIKEEVRQRALALDEA 5990
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESkldelaeelaeLEEKLEELKEElesleaELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5991 VSQSTQFHDKIEPMLETLENLSSRL---------RMPPLIPAEVDKIRECISDNKSatvELEKLQPSFEALKRRGEELIG 6061
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELRE 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6062 RSQGADKDL-AAKEIQDKLDQMVFFWEDIKARAEE--REIKFL---------------DVLELAEKFwydMAALLTTI-K 6122
Cdd:TIGR02168  469 ELEEAEQALdAAERELAQLQARLDSLERLQENLEGfsEGVKALlknqsglsgilgvlsELISVDEGY---EAAIEAALgG 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6123 DTQDIVHDLESpgidpsiikQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPE-----VRKSIDEMNNAWEN 6197
Cdd:TIGR02168  546 RLQAVVVENLN---------AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgVAKDLVKFDPKLRK 616
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6198 LNKTWKERL---EKLEDAMQAAVQYQdtLQAMFDWLDNTVIK---LCTMPPVGTDLNTV------KDQLNEMKEFKVEVY 6265
Cdd:TIGR02168  617 ALSYLLGGVlvvDDLDNALELAKKLR--PGYRIVTLDGDLVRpggVITGGSAKTNSSILerrreiEELEEKIEELEEKIA 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6266 QQQIEMEKLNHQGELMLKKATD-ETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEELMSWLTHTE 6344
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6345 ELLDAQrpisgdpkviEVELAKhhvLKNDVLAHQATVETVNKAGNELLE--SSAGDDASSLRSRLEAMNQCWESVLQKTE 6422
Cdd:TIGR02168  775 EELAEA----------EAEIEE---LEAQIEQLKEELKALREALDELRAelTLLNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 6423 EREQQLQSTLQQAQGFHSEIEDFLLELTRMESQL-SASKptggLPETAREQLDTHMELYSQLKAKEETYNQ 6492
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELeALLN----ERASLEEALALLRSELEELSEELRELES 908
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5964-6493 3.41e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5964 EKYQKAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRmppLIPAEVDKIRECISDNKSATVELE 6043
Cdd:PRK03918   158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN---EISSELPELREELEKLEKEVKELE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6044 KLQPSFEALKRRGEELIGRSQGADKDLaaKEIQD----------KLDQMVFFWEDIKARAEEREI------KFLDVLELA 6107
Cdd:PRK03918   235 ELKEEIEELEKELESLEGSKRKLEEKI--RELEErieelkkeieELEEKVKELKELKEKAEEYIKlsefyeEYLDELREI 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6108 EKfwyDMAALLTTIKDTQDIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLifacGETEKPEVRKS 6187
Cdd:PRK03918   313 EK---RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL----ERLKKRLTGLT 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6188 IDEMNNAWENLNKtwkeRLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIKL----CTMPPVGTDLnTVKDQLNEMKEFKVE 6263
Cdd:PRK03918   386 PEKLEKELEELEK----AKEEIEEEISKITARIGELKKEIKELKKAIEELkkakGKCPVCGREL-TEEHRKELLEEYTAE 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6264 VYQQQIEMEKLNHQgELMLKKATDETDRDIIREP-LTELKHLWENLGEKiahrQHKLEGallalgqfqHALEELMSWLTH 6342
Cdd:PRK03918   461 LKRIEKELKEIEEK-ERKLRKELRELEKVLKKESeLIKLKELAEQLKEL----EEKLKK---------YNLEELEKKAEE 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6343 TEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNEL---LESSAGDDASSLRSRLEAMNQCW----- 6414
Cdd:PRK03918   527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeLEELGFESVEELEERLKELEPFYneyle 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6415 ----ESVLQKTEEREQQLQSTLQQAQgfhSEIEDFLLELTRMESQLSASKPTGGlPETAREQLDTHMELYSQLKAKEETY 6490
Cdd:PRK03918   607 lkdaEKELEREEKELKKLEEELDKAF---EELAETEKRLEELRKELEELEKKYS-EEEYEELREEYLELSRELAGLRAEL 682

                   ...
gi 2020023496 6491 NQL 6493
Cdd:PRK03918   683 EEL 685
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
45-171 3.67e-05

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: 46.18  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496   45 KTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGIKLEpaglktlrlvsmpswchtnneeqaeeDDDDVPRE 122
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVE--------------------------DINGCPRS 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2020023496  123 KGRMrfhrLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTI 171
Cdd:cd21286     57 QSQM----IENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2287-2325 3.74e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 44.24  E-value: 3.74e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2287 VLSAQLLDGGIFHEQTGQKLLLNEAISRGIVPSHTAVKL 2325
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
3631-3943 4.06e-05

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: 50.15  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3631 ALAGHQGRTTQQDLSALQKNQSDLKDLQDDIQNRATSFATVVKDIEgfmeenqtklspRELTALREKLHQAKEQYEALQE 3710
Cdd:COG4942     16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAALEA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3711 ETRVAQKELEEavtsalqqetekskAAKELAENKKKIDALLDWVtsvgssggQLLTNLPGMEQLSGASlekGALDTTDGY 3790
Cdd:COG4942     84 ELAELEKEIAE--------------LRAELEAQKEELAELLRAL--------YRLGRQPPLALLLSPE---DFLDAVRRL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3791 MGVNQAPEKLDKQCEMMKARHQELLSQQQNFILATQSAQAFLDqhghnltpeEQQMLQQKLGELKEQYSTSLAQSEAELK 3870
Cdd:COG4942    139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA---------ELEEERAALEALKAERQKLLARLEKELA 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3871 QVQTLQDELQKFLQDHKEFESWLERSEKELENMHKGGSSPE---TLP-----SLLKRQGSFSEDVISHKGdlrfVTISGQ 3942
Cdd:COG4942    210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAlkgKLPwpvsgRVVRRFGERDGGGGRNKG----IDIAAP 285

                   .
gi 2020023496 3943 K 3943
Cdd:COG4942    286 P 286
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6105-6211 4.16e-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: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6105 ELAEKFWYDMAALLTTIKDTQDIVHDlESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFAcGETEKPEV 6184
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 2020023496 6185 RKSIDEMNNAWENLNKTWKERLEKLED 6211
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3561-3752 4.31e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3561 QQNRQMLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVktlqkqqntcHQQLEDLcSW----VGQAERALAghq 3636
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA----------LQRLAEY-SWdeidVASAEREIA--- 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3637 grTTQQDLSALQKNQSDLKDLQDDIQNRATSFATVVKDIEGfMEENQTKLSpRELTALREKLHQAKEQYEALQEETRVAQ 3716
Cdd:COG4913    672 --ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE-LKGEIGRLE-KELEQAEEELDELQDRLEAAEDLARLEL 747
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2020023496 3717 KE-LEEAVTSALQQETEKsKAAKELAENKKKIDALLD 3752
Cdd:COG4913    748 RAlLEERFAAALGDAVER-ELRENLEERIDALRARLN 783
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5834-6495 4.95e-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: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5834 ELFSHRSEIFGTcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLPSP 5913
Cdd:TIGR02168  289 ELYALANEISRL--EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5914 AID-HEQLRQQQEEMRQLRESIAEHKPHIDKLLK----IGPQLKELNPEEGEMVEEKYQKAENMYAQIKEEVRQRALALD 5988
Cdd:TIGR02168  367 LEElESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5989 EAVSQSTQFHDKIEPMLETLEnlssrlrmpplipAEVDKIRECISDNKSatvELEKLQPSFEALKRRGEELIGRSQGADK 6068
Cdd:TIGR02168  447 EELEELQEELERLEEALEELR-------------EELEEAEQALDAAER---ELAQLQARLDSLERLQENLEGFSEGVKA 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6069 DLAAKEIQDKLDQMVffWEDIKARAE-EREI-----KFLD--VLELAEKFWYDMAAL------------LTTIKDTQDIV 6128
Cdd:TIGR02168  511 LLKNQSGLSGILGVL--SELISVDEGyEAAIeaalgGRLQavVVENLNAAKKAIAFLkqnelgrvtflpLDSIKGTEIQG 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6129 HDLESP-------GIDPSIIKQQVEA-------------AETIKEETDGLHEELEFIRI--LGADLIFACG----ETEKP 6182
Cdd:TIGR02168  589 NDREILkniegflGVAKDLVKFDPKLrkalsyllggvlvVDDLDNALELAKKLRPGYRIvtLDGDLVRPGGvitgGSAKT 668
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6183 -----EVRKSIDEmnnAWENLNKTwKERLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIKLctmppvGTDLNTVKDQLnEM 6257
Cdd:TIGR02168  669 nssilERRREIEE---LEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL------SRQISALRKDL-AR 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6258 KEFKVEVYQQQIEMEKLNhQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEEL- 6336
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLn 816
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6337 MSWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLE---------SSAGDDASSLRSRL 6407
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnerASLEEALALLRSEL 896
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6408 EAMnqcwESVLQKTEEREQQLQSTLQQAQgfhSEIEDFLLELTRMESQLSaskptgGLPETAREQLDTHMELYSQLKAKE 6487
Cdd:TIGR02168  897 EEL----SEELRELESKRSELRRELEELR---EKLAQLELRLEGLEVRID------NLQERLSEEYSLTLEEAEALENKI 963

                   ....*...
gi 2020023496 6488 ETYNQLLD 6495
Cdd:TIGR02168  964 EDDEEEAR 971
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1651-1689 5.27e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 5.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 1651 ILEAHLATGGFSLSPSENCINLEEAFHQGLISAWLHSVL 1689
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3569-4282 5.42e-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: 50.45  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3569 LLNELQRSFQDIlEQTAAQVDALQGHLQQMEQEalvktLQKQQNTCHQqLEDLCSWVGQAERALAGHQGRTTQQDLSALQ 3648
Cdd:TIGR02169  228 LLKEKEALERQK-EAIERQLASLEEELEKLTEE-----ISELEKRLEE-IEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3649 KNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENQTKL--SPRELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSA 3726
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeeLEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3727 -------LQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLLTNLPGMEQlsgaslEKGALDTtdgymgvnqapEK 3799
Cdd:TIGR02169  381 aetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA------KINELEE-----------EK 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3800 LDKQCEMMKARhQELLSQQQnfILATQSAQAFLDQHGHNLTPEEQQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDEL 3879
Cdd:TIGR02169  444 EDKALEIKKQE-WKLEQLAA--DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3880 QKFLQDHKEFESWLERSEKELE-------------------------NMHKGG----------SSPETLPSLLKRQG--S 3922
Cdd:TIGR02169  521 QGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddavakeaiellKRRKAGratflplnkmRDERRDLSILSEDGviG 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3923 FSEDVIS---------------------------HKGDLRFVTISGQkVLDMENSFKEGKEPSEIGNLVKDKLKDATERy 3975
Cdd:TIGR02169  601 FAVDLVEfdpkyepafkyvfgdtlvvedieaarrLMGKYRMVTLEGE-LFEKSGAMTGGSRAPRGGILFSRSEPAELQR- 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3976 taLHSKCTRLGSHLNMLLGQYHQFQNSADSLQAWMQACEANVEKLLSDTVAsdpgvLQEQLATTKQLQEELAEHQVPVE- 4054
Cdd:TIGR02169  679 --LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-----LEQEEEKLKERLEELEEDLSSLEq 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4055 KLQKVARDIMEIEGEPAPDHRHVQETTDSILSHFQSLSyslaerSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLEGKQ 4134
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4135 vsslssgvIQEALATnmKLKQDIARQKSSLEATREMVTRFMETadsttaavLQGKLAEVSQRFEQLCLQQQEKESSLKKL 4214
Cdd:TIGR02169  826 --------LEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIEN--------LNGKKEELEEELEELEAALRDLESRLGDL 887
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 4215 lpqAEMFEHLSGKLQQfMENKSRMLASgnqpdqDITHFFQQIQELNLEMEDQQENLDTLEHLVTELSS 4282
Cdd:TIGR02169  888 ---KKERDELEAQLRE-LERKIEELEA------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
4645-5143 7.16e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 7.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4645 DVSLSTSQVQKELQSINQKwvELTDKLNSRSSQIDQAIVKSTQYQEllqdlsEKVRAVGQRLSVQSAIstqpEAVKQQLE 4724
Cdd:PRK02224   184 DQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEE------QREQARETRDEADEVL----EEHEERRE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4725 ETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQY-----LKDELKKRLETValplqGLEDLAADRINRLQAALASTQqfq 4799
Cdd:PRK02224   252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRerleeLEEERDDLLAEA-----GLDDADAEAVEARREELEDRD--- 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4800 qmfDELRTWLDD-KQSQQAKNCPIsaklERLQSQLQENEEFQKSLNQHSGSYEVIVAEGEslllsvppgEEKRTLQNQLV 4878
Cdd:PRK02224   324 ---EELRDRLEEcRVAAQAHNEEA----ESLREDADDLEERAEELREEAAELESELEEAR---------EAVEDRREEIE 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4879 ELKNHWEELSKKTADRQSRLKDCmqkaqkyQWHVEDLVPWIEDCKAKMSELRVTLDPVQlessllrskamlNEVEKRRSL 4958
Cdd:PRK02224   388 ELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELREREAELEATLRTAR------------ERVEEAEAL 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4959 LEILN--SAADILINSSEADEDGIRDEKAGinqNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAkhqleif 5036
Cdd:PRK02224   449 LEAGKcpECGQPVEGSPHVETIEEDRERVE---ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR------- 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5037 dalgsqacsnKNLEKLRAQQ-EVLQALEPQVDYLRNFTQGLVEDAPDGSDASQllhQAEVAQQEFLEVKQRVNSGCVMME 5115
Cdd:PRK02224   519 ----------EDLEELIAERrETIEEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELK 585
                          490       500
                   ....*....|....*....|....*...
gi 2020023496 5116 NKLEGIGqfhcRVREMFSQLADLDDELD 5143
Cdd:PRK02224   586 ERIESLE----RIRTLLAAIADAEDEIE 609
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5894-5989 7.17e-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: 45.39  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5894 EELSPWIEETRALIAQLPSPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQKAENMY 5973
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
                           90
                   ....*....|....*.
gi 2020023496 5974 AQIKEEVRQRALALDE 5989
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4903-5007 7.39e-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: 45.39  E-value: 7.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4903 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRD 4982
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 2020023496 4983 EKAGINQNMDAVTEELQAKTGSLEE 5007
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
5554-6016 7.63e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.95  E-value: 7.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5554 QALSNAR-LFGEDEVEVLN---WLAEVEDKLSSV--FVKDFKQ-----DVLHRQHADHLALNEEI---VNRkknvDQAIK 5619
Cdd:COG3096    420 QALEKARaLCGLPDLTPENaedYLAAFRAKEQQAteEVLELEQklsvaDAARRQFEKAYELVCKIageVER----SQAWQ 495
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5620 NGQALLKQTTGEEVLLiqEKLDGIKTRYADItvtsSKALRTLEQARQLATKFQ-------STYEELTGWLREVEEELAT- 5691
Cdd:COG3096    496 TARELLRRYRSQQALA--QRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCqrigqqlDAAEELEELLAELEAQLEEl 569
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5692 SGGQSPTGEQIPQFQQRQKELKKEVMEHRlvldtvnevSRALLelvpWR-AREGLDKL-------VSDANE--------- 5754
Cdd:COG3096    570 EEQAAEAVEQRSELRQQLEQLRARIKELA---------ARAPA----WLaAQDALERLreqsgeaLADSQEvtaamqqll 636
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5755 ----QYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAELAWVAET-KRKLMA-----------------LGPIR---LEQD 5809
Cdd:COG3096    637 ererEATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERlGGVLLSeiyddvtledapyfsalYGPARhaiVVPD 716
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5810 QTTAQLQVQK----------------AFSiDIIRHKDSMDEL-----------FSHRSEI--FGTCGEEQK-TVLQEKTE 5859
Cdd:COG3096    717 LSAVKEQLAGledcpedlyliegdpdSFD-DSVFDAEELEDAvvvklsdrqwrYSRFPEVplFGRAAREKRlEELRAERD 795
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5860 SLIQQY----------------------------------EAISLLNSERY---ARLERAQVLVNQFWETYEELSPWIEE 5902
Cdd:COG3096    796 ELAEQYakasfdvqklqrlhqafsqfvgghlavafapdpeAELAALRQRRSeleRELAQHRAQEQQLRQQLDQLKEQLQL 875
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5903 TRALIAQLPSPAIDH-----EQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKElNPEEGEMVEEKYQKAEnmyaQIK 5977
Cdd:COG3096    876 LNKLLPQANLLADETladrlEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQS-DPEQFEQLQADYLQAK----EQQ 950
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 2020023496 5978 EEVRQRALALDEAVSQSTQF-HDKIEPMLETLENLSSRLR 6016
Cdd:COG3096    951 RRLKQQIFALSEVVQRRPHFsYEDAVGLLGENSDLNEKLR 990
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
185-294 9.94e-05

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: 45.18  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  185 ESGDMSAKEKLLLWTQKvtaGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGV 262
Cdd:cd21312      7 EAKKQTPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGI 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2020023496  263 TRLLDAEDVDVPSPDEKSVITYVSSiydaFPK 294
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQ----FPK 111
PLEC smart00250
Plectin repeat;
2681-2718 1.24e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 1.24e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2020023496  2681 LKVLEAQANTGGIIDTATGKRLTLASALEEKLVDENMV 2718
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
EF-hand_8 pfam13833
EF-hand domain pair;
7158-7207 1.37e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 43.07  E-value: 1.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2020023496 7158 QDGKITRQEFIDGILASKFP-TTKLEMTAVADIFDRDGDGYIDYYEFVAAL 7207
Cdd:pfam13833    1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3524-3901 1.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3524 QQYEDLKQPMAERKAQLDALAfdiqffisehaqdlspqqnrqmLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEal 3603
Cdd:COG1196    213 ERYRELKEELKELEAELLLLK----------------------LRELEAELEELEAELEELEAELEELEAELAELEAE-- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3604 VKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRTTQQDLSALQKNQSDLKDLQDDIQnratsfatvvkdiegfmeenq 3683
Cdd:COG1196    269 LEELRLELEELELELEEA-----QAEEYELLAELARLEQDIARLEERRRELEERLEELE--------------------- 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3684 tklspRELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDwvtsvgssggQ 3763
Cdd:COG1196    323 -----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----------E 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3764 LLTNLpgMEQLSGASLEKGALdttdgymgvnQAPEKLDKQCEMMKARHQELLSQQQNFILATQSAQAFLdqhghnltpEE 3843
Cdd:COG1196    388 LLEAL--RAAAELAAQLEELE----------EAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------EE 446
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023496 3844 QQMLQQKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFESWLERSEKELE 3901
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4032-4871 2.29e-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: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4032 LQEQLA-TTKQLQEELAEHQVPVEKLQKVARDIMEIEGEPApdhRHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQ 4110
Cdd:TIGR02169  249 LEEELEkLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4111 SVQESLESLLQSIGEVEQNLEGKQVSSLS-SGVIQEALATNMKLKQDIARQKSSLEATREmvtrfmetadsttaavlqgK 4189
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRD-------------------E 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4190 LAEVSQRFEQLclqQQEKESSLKKLLPQAEMFEHLSGKLQQFmenksrmlasgnqpDQDITHFFQQIQELNLEMEDQQEN 4269
Cdd:TIGR02169  387 LKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADL--------------NAAIAGIEAKINELEEEKEDKALE 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4270 LDTLEhlvTELSScgFALDLCQHQDRVQNLRKDFTELqktvkerEKDASSCQEQLDEFRKLVRTFQkwlkETEGSIPPTE 4349
Cdd:TIGR02169  450 IKKQE---WKLEQ--LAADLSKYEQELYDLKEEYDRV-------EKELSKLQRELAEAEAQARASE----ERVRGGRAVE 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4350 tsmsaKELEKQIEHLKSLLDDWASKG----TLVEeiNCKGTSLENLIMEITA---------PDSQGKTGSILP------- 4409
Cdd:TIGR02169  514 -----EVLKASIQGVHGTVAQLGSVGeryaTAIE--VAAGNRLNNVVVEDDAvakeaiellKRRKAGRATFLPlnkmrde 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4410 SVGSSVGSVNGYhtckdlTEIQCDMSDVNLKYEK-----LGG-VLHERQESLQAILNRMEEVHKEAnsvlqwleskeEVL 4483
Cdd:TIGR02169  587 RRDLSILSEDGV------IGFAVDLVEFDPKYEPafkyvFGDtLVVEDIEAARRLMGKYRMVTLEG-----------ELF 649
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4484 KSMDAMSSPTKTEtvKAQAESNKAFLAELEQNSPKIQKVKEALAGLLvtypnsQEAENWKKIQEELNSRWERATEVTVAR 4563
Cdd:TIGR02169  650 EKSGAMTGGSRAP--RGGILFSRSEPAELQRLRERLEGLKRELSSLQ------SELRRIENRLDELSQELSDASRKIGEI 721
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4564 QRQLEESASHLACFQAAESQLRPWLMEKElmmgvlgplsidpNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGP 4643
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLE-------------QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4644 GDVSLstSQVQKELQSINqkwvELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEkvravgQRLSVQSAISTQPEAVKQQL 4723
Cdd:TIGR02169  789 SHSRI--PEIQAELSKLE----EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ------ELQEQRIDLKEQIKSIEKEI 856
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4724 EetsEIRSDLEQLDHEVKEAQ----TLCDELSVLIGEqylKDELKKRLETVALPLQGLE---DLAADRINRLQAALastq 4796
Cdd:TIGR02169  857 E---NLNGKKEELEEELEELEaalrDLESRLGDLKKE---RDELEAQLRELERKIEELEaqiEKKRKRLSELKAKL---- 926
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4797 qfQQMFDELRTWLDDKQSQQAKNCP------ISAKLERLQSQL-----------QENEEFQKSLNQHSGSYEVIVAEGES 4859
Cdd:TIGR02169  927 --EALEEELSEIEDPKGEDEEIPEEelsledVQAELQRVEEEIralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKA 1004
                          890
                   ....*....|..
gi 2020023496 4860 LLLSVPPGEEKR 4871
Cdd:TIGR02169 1005 ILERIEEYEKKK 1016
SPEC smart00150
Spectrin repeats;
3880-3990 2.31e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 2.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  3880 QKFLQDHKEFESWLERSEKELENMHKGGsSPETLPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDMENSFKEgkepse 3959
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE------ 73
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2020023496  3960 ignLVKDKLKDATERYTALHSKCTRLGSHLN 3990
Cdd:smart00150   74 ---EIEERLEELNERWEELKELAEERRQKLE 101
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
5624-6354 2.34e-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: 48.43  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5624 LLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFQ--STYEELTGWLREVEEELATsggqsptgeQ 5701
Cdd:TIGR00618  205 LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRA---------Q 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5702 IPQFQQRQKELKKEVMEHRLVLDTvnevsrALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRS---- 5777
Cdd:TIGR00618  276 EAVLEETQERINRARKAAPLAAHI------KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqt 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5778 -----QQYEQAADAELAWVAETKRKLMALGPIR-LEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRSEifgtCGEEQK 5851
Cdd:TIGR00618  350 lhsqeIHIRDAHEVATSIREISCQQHTLTQHIHtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF----RDLQGQ 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5852 TVLQEKTESLIQQYEAISLLNSERYARLERAQ-VLVNQFWETYEELSPWIEETRALIAQLPSPAIDHEQ-LRQQQEEMRQ 5929
Cdd:TIGR00618  426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLArLLELQEEPCP 505
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5930 LRESIAEHKPHIDKLLKIGPQLKELnpEEGEMVEEKYQKA-ENMYAQIKEEVRQRAL------ALDEAVSQSTQFHDKIE 6002
Cdd:TIGR00618  506 LCGSCIHPNPARQDIDNPGPLTRRM--QRGEQTYAQLETSeEDVYHQLTSERKQRASlkeqmqEIQQSFSILTQCDNRSK 583
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6003 PMLETLENLSSRLRmpPLIPAEVdkiRECISDNKSATVELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQDKLDQm 6082
Cdd:TIGR00618  584 EDIPNLQNITVRLQ--DLTEKLS---EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ- 657
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6083 vffwedikaraEEREIKFLDVLELAEKFWYDMAALLTtikdtqdivhdlespgidpsiikqqveAAETIKEETDGLHEEL 6162
Cdd:TIGR00618  658 -----------ERVREHALSIRVLPKELLASRQLALQ---------------------------KMQSEKEQLTYWKEML 699
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6163 EFIrilgaDLIFACGETEKPEVRKSIDEmnnaWENLNKTWKERLEKLEDAMQaavQYQDTLQAMFDWL--DNTVIKLCTM 6240
Cdd:TIGR00618  700 AQC-----QTLLRELETHIEEYDREFNE----IENASSSLGSDLAAREDALN---QSLKELMHQARTVlkARTEAHFNNN 767
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6241 PPVGTDLNTvkdqLNEMKEFKVEVYQQQIEMEKLnhQGELMLKKATDETDRDiirEPLTELKHLWENLGEKIAHRQHKLE 6320
Cdd:TIGR00618  768 EEVTAALQT----GAELSHLAAEIQFFNRLREED--THLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRLE 838
                          730       740       750
                   ....*....|....*....|....*....|....
gi 2020023496 6321 GALLALGQFQHALEELMSWLTHTEELLDAQRPIS 6354
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKII 872
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5879-6109 2.39e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5879 LERAQVLVNQFWETYEELSPWIEETRALIAQLPSPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 5958
Cdd:PRK03918   185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5959 GEMVEEKYQKAENMYAQIKE--EVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRmpplipaevdKIRECISDNK 6036
Cdd:PRK03918   265 EERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----------GIEERIKELE 334
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 6037 SATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 6109
Cdd:PRK03918   335 EKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
5848-6095 2.72e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.91  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5848 EEQKTVLQEKTESLIQQYEAisllNSERYARLE------RAQVLVN--QFWETYEELSPWIEETRALIAQL--------P 5911
Cdd:PRK04778   118 EEDIEQILEELQELLESEEK----NREEVEQLKdlyrelRKSLLANrfSFGPALDELEKQLENLEEEFSQFveltesgdY 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5912 SPAidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGP-QLKELnpEEG--EMVEEKY----QKAENMYAQIKEEVRQ-- 5982
Cdd:PRK04778   194 VEA--REILDQLEEELAALEQIMEEIPELLKELQTELPdQLQEL--KAGyrELVEEGYhldhLDIEKEIQDLKEQIDEnl 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5983 ---RALALDEAVSQSTQFHDKIEPMLETLEN-LSSRLRMPPLIPAEVDKIRECISDNKSATVELEKLQPSFE-------- 6050
Cdd:PRK04778   270 allEELDLDEAEEKNEEIQERIDQLYDILEReVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTlneseles 349
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 6051 --ALKRRGEELIGRSQGADKDLAAK-----EIQDKLDQMVFFWEDIKARAEE 6095
Cdd:PRK04778   350 vrQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEK 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5376-6163 2.84e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5376 KAQIQEQKLLQRLLDDRKATVDMLQAEggriaqsAELADREKITGQLESLESRWTELLSKAAARQKQLEDILVLAKQFHE 5455
Cdd:TIGR02169  207 REKAERYQALLKEKREYEGYELLKEKE-------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5456 TAEPISDFLSVTekklansepVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQS-LSSLTSPAEQgvLSEKIDSL 5534
Cdd:TIGR02169  280 KIKDLGEEEQLR---------VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAeIDKLLAEIEE--LEREIEEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5535 QARYSEIQDRCCRKAALLDQALSNArlfGEDEVEvlnwLAEVEDKLSSVFVKdfkQDVLHRQHADHLALNEEIVNRKKNV 5614
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAEL---EEVDKE----FAETRDELKDYREK---LEKLKREINELKRELDRLQEELQRL 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5615 DQAIKNGQALLKQttgeevllIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFQSTYEELTGWLREVEEELatsgg 5694
Cdd:TIGR02169  419 SEELADLNAAIAG--------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL----- 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5695 qSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEvsrallelvpwrAREGLDKLVSD---ANEQYKL-VSDTIGQRVDEI 5770
Cdd:TIGR02169  486 -SKLQRELAEAEAQARASEERVRGGRAVEEVLKA------------SIQGVHGTVAQlgsVGERYATaIEVAAGNRLNNV 552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5771 ----DAAIQRSQQY---EQAADAELAWVAETKRKLMALGPIRLEQ------DQTTAQLQVQKAFSI---------DIIRH 5828
Cdd:TIGR02169  553 vvedDAVAKEAIELlkrRKAGRATFLPLNKMRDERRDLSILSEDGvigfavDLVEFDPKYEPAFKYvfgdtlvveDIEAA 632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5829 KDSMD---------ELFSHRSEIFG-----TCGEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYE 5894
Cdd:TIGR02169  633 RRLMGkyrmvtlegELFEKSGAMTGgsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5895 ELSPWIEETRALIAQLpspAIDHEQLRQQQEEMR----QLRESIAEHKPHIDKL--------LKIGPQLKELNPEEGEMV 5962
Cdd:TIGR02169  713 DASRKIGEIEKEIEQL---EQEEEKLKERLEELEedlsSLEQEIENVKSELKELearieeleEDLHKLEEALNDLEARLS 789
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5963 EEKYQKAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRmppLIPAEVDKIRECISDNKSatvEL 6042
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI---DLKEQIKSIEKEIENLNG---KK 863
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6043 EKLQPSFEALKRRGEELIGRSQGADKDLaaKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEKFWYDMAALLTTIK 6122
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRLGDLKKER--DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|.
gi 2020023496 6123 DtqdivhDLESPGIDPSIikqqveaaETIKEETDGLHEELE 6163
Cdd:TIGR02169  942 E------DEEIPEEELSL--------EDVQAELQRVEEEIR 968
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
7150-7208 2.89e-04

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 45.28  E-value: 2.89e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7150 FFRRIDKDQDGKITRQEfIDGILASKFPTTKLEMTA-VADIFDRDGDGYIDYYEFvAALH 7208
Cdd:cd16185      5 WFRAVDRDRSGSIDVNE-LQKALAGGGLLFSLATAEkLIRMFDRDGNGTIDFEEF-AALH 62
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
3375-4131 2.93e-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: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3375 SLLRNIEMRTKQIQPLELNLAELQDLLCQAK-VLERELKDLTTLVSQElecvnqiiisqpQEVPAQLLKALEKDAKNLQK 3453
Cdd:TIGR00618  191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKqVLEKELKHLREALQQT------------QQSHAYLTQKREAQEEQLKK 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3454 slssvsdtwnSRLLHFQNAVEIEKTKVLNQHTQLEGRLQDLRAWVgnkNLILNSKgsnseidvdSLNLCLQQYEDLKQPM 3533
Cdd:TIGR00618  259 ----------QQLLKQLRARIEELRAQEAVLEETQERINRARKAA---PLAAHIK---------AVTQIEQQAQRIHTEL 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3534 AERKAQLDALafdIQFFISEHAQDLSPQQNRQmlrLLNELQRSFQDILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNT 3613
Cdd:TIGR00618  317 QSKMRSRAKL---LMKRAAHVKQQSSIEEQRR---LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3614 CHQQLEDLCSWVGQaERALAgHQGRTTQQDLSALQKNQSDLKDLQDDIQNRAtsfatvvkdiegfmeENQTKLSPRELTA 3693
Cdd:TIGR00618  391 LTQKLQSLCKELDI-LQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYA---------------ELCAAAITCTAQC 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3694 LREKLHQAKEQYEALQEEtrvaqKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLLTNLPGMEQ 3773
Cdd:TIGR00618  454 EKLEKIHLQESAQSLKER-----EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3774 LSGASLekgaldttDGYMGVNQAPEKLDKQCEMMKARHQELLSQ----QQNFILATQSAQAFLDQhgHNLTPEEQQMLQQ 3849
Cdd:TIGR00618  529 RMQRGE--------QTYAQLETSEEDVYHQLTSERKQRASLKEQmqeiQQSFSILTQCDNRSKED--IPNLQNITVRLQD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3850 KLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHKEFEswlersEKELENMHKGGSSpETLPSLLKRQGSFSEDVIs 3929
Cdd:TIGR00618  599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ------ELALKLTALHALQ-LTLTQERVREHALSIRVL- 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3930 hkgdlrfvtisgQKVLDMENSFKEGKEPSEIGNLVKDKlKDATERYTALHSKCTRLGShlnmLLGQYHQFQNSADSLQAW 4009
Cdd:TIGR00618  671 ------------PKELLASRQLALQKMQSEKEQLTYWK-EMLAQCQTLLRELETHIEE----YDREFNEIENASSSLGSD 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4010 MQACEANVEKLLSDTVASDPGVLQEQ-LATTKQLQEELAEHQVpVEKLQKVARDIMEIEGEPAPDhrhVQETTDSILSHF 4088
Cdd:TIGR00618  734 LAAREDALNQSLKELMHQARTVLKARtEAHFNNNEEVTAALQT-GAELSHLAAEIQFFNRLREED---THLLKTLEAEIG 809
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|...
gi 2020023496 4089 QSLSYSLAERSSLLQKAIAQSQSVQESLESLLQSIGEVEQNLE 4131
Cdd:TIGR00618  810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2401-2432 3.91e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 41.16  E-value: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2401 ILERQVVTGGIIDLKRGKKVSVTLASTLGLVD 2432
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLID 32
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
5173-5814 4.39e-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: 47.66  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5173 KLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLNDATTAAEEAEA 5252
Cdd:TIGR00618  195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRA 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5253 LQWVVGTEVEIINQQLadfkmfQKEQVDPLQMKLQQVNGLGQGLIQsagkdcDVQGLEHDMEEINARWNTLNKKVAQRIA 5332
Cdd:TIGR00618  275 QEAVLEETQERINRAR------KAAPLAAHIKAVTQIEQQAQRIHT------ELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5333 Q---LQEALLHCGKFQDALEPLLSWLADTEELIANQKPpsaeykvVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAqs 5409
Cdd:TIGR00618  343 QrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-------IHTLQQQKTTLTQKLQSLCKELDILQREQATID-- 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5410 AELADREKITGQLESLESrwTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEK--KLANSEPVGTQTAKIQ-- 5485
Cdd:TIGR00618  414 TRTSAFRDLQGQLAHAKK--QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqQLQTKEQIHLQETRKKav 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5486 --QQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQGV-----LSEKIDSLQARYSEIQDRCCR---KAALLDQA 5555
Cdd:TIGR00618  492 vlARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEqtyaqLETSEEDVYHQLTSERKQRASlkeQMQEIQQS 571
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5556 LSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHR--QHADHLALNEEIVN-RKKNVDQAIKNGQALLKQT-TGE 5631
Cdd:TIGR00618  572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAceQHALLRKLQPEQDLqDVRLHLQQCSQELALKLTAlHAL 651
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5632 EVLLIQEKLdgiktRYADITVTSSKAlRTLEQARQLATKFQSTYEELTGWLREVEE-ELATSGGQSPTGEQIPQFQQRQK 5710
Cdd:TIGR00618  652 QLTLTQERV-----REHALSIRVLPK-ELLASRQLALQKMQSEKEQLTYWKEMLAQcQTLLRELETHIEEYDREFNEIEN 725
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5711 ELKKEVMEHRLVLDTVNEVSRALLELVPWRAREglDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAELAW 5790
Cdd:TIGR00618  726 ASSSLGSDLAAREDALNQSLKELMHQARTVLKA--RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT 803
                          650       660
                   ....*....|....*....|....*
gi 2020023496 5791 V-AETKRKLMALGPIRLEQDQTTAQ 5814
Cdd:TIGR00618  804 LeAEIGQEIPSDEDILNLQCETLVQ 828
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4153-4485 4.56e-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: 47.37  E-value: 4.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4153 LKQDIARQKSSL-EATREM--VTRFMETAdSTTAAVLQGKLAEVSQRFEQLCLQQQEKEsslKKLLPQAEMFEHLSGKLQ 4229
Cdd:TIGR02169  693 LQSELRRIENRLdELSQELsdASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4230 QFMENKSRMLASGNQPDQDITHffQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLCQHQDRVQNLRKDFTELQKT 4309
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQEQ 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4310 VKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMsaKELEKQIEHLKSLLDDWASK-GTLVEEINCKG--- 4385
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--GDLKKERDELEAQLRELERKiEELEAQIEKKRkrl 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4386 ----TSLENLIMEITAPDSQGKTGSILPSVGSSVGSVngYHTCKDLTEIQCDMSDVNLKYEKLGGVLHERQESLQAILNR 4461
Cdd:TIGR02169  920 selkAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
                          330       340
                   ....*....|....*....|....
gi 2020023496 4462 MEEvhkEANSVLQWLESKEEVLKS 4485
Cdd:TIGR02169  998 LEE---ERKAILERIEEYEKKKRE 1018
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
5757-6224 4.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5757 KLVSDTIGQRVDEIDAAIQ--RSQQY-EQAADAELawvaetkrklmalGPIRLEQDQTTAQLQVQKafSIDIIRHKDSMD 5833
Cdd:PRK02224   142 KLINATPSDRQDMIDDLLQlgKLEEYrERASDARL-------------GVERVLSDQRGSLDQLKA--QIEEKEEKDLHE 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5834 ELFSHRSEIFGTCG-----EEQKTVLQE---KTESLIQQYE------------------AISLLNSERYARLERAQVLVn 5887
Cdd:PRK02224   207 RLNGLESELAELDEeieryEEQREQAREtrdEADEVLEEHEerreeletleaeiedlreTIAETEREREELAEEVRDLR- 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5888 qfwETYEELSpwiEETRALIAQLPSPAIDHEQLRQQQEEMR----QLRESIAEHKPHIDKLLkigpqlkelnpEEGEMVE 5963
Cdd:PRK02224   286 ---ERLEELE---EERDDLLAEAGLDDADAEAVEARREELEdrdeELRDRLEECRVAAQAHN-----------EEAESLR 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5964 EKYQKAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNKSATVELE 6043
Cdd:PRK02224   349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6044 K-LQPSFEALKRR---GEELI--GRSQGADKDL-------AAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEkf 6110
Cdd:PRK02224   429 AeLEATLRTARERveeAEALLeaGKCPECGQPVegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-- 506
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6111 wydMAALLTTIKDTQDIVHDLESpgIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLifacgETEKPEVRKSIDE 6190
Cdd:PRK02224   507 ---AEDRIERLEERREDLEELIA--ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-----EEEAEEAREEVAE 576
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2020023496 6191 MNNAWENLNKTwKERLEKLEDAMQAAVQYQDTLQ 6224
Cdd:PRK02224   577 LNSKLAELKER-IESLERIRTLLAAIADAEDEIE 609
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
44-88 5.56e-04

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: 43.03  E-value: 5.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2020023496   44 KKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLE 88
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLE 47
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
3524-3750 6.33e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3524 QQYEDLKQPMAERKAQLDALAFDIQ----------FFISEH---AQDLSPQQNRQMLRL-LNELQR---SFQDILEQTAA 3586
Cdd:COG3096    785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsQFVGGHlavAFAPDPEAELAALRQrRSELERelaQHRAQEQQLRQ 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3587 QVDALQGHLQQME----QEALVK--TLQKQQNTCHQQLEDLcswvGQAERALAGHQGRTTQ------------QDLSALQ 3648
Cdd:COG3096    865 QLDQLKEQLQLLNkllpQANLLAdeTLADRLEELREELDAA----QEAQAFIQQHGKALAQleplvavlqsdpEQFEQLQ 940
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3649 KNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENqtklSPRELT---ALREKLHQAKEQYEALQEETRVAQKELEEAVTS 3725
Cdd:COG3096    941 ADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYED----AVGLLGensDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
                          250       260
                   ....*....|....*....|....*....
gi 2020023496 3726 ALQ--QETEKSKAAK--ELAENKKKIDAL 3750
Cdd:COG3096   1017 YNQvlASLKSSRDAKqqTLQELEQELEEL 1045
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4547-5106 7.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4547 EELNSRWERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKELmmgvlgplsidpnMLNAQKQQVQFMLKEFEARR 4626
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------------ELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4627 QQHEQLNEAAQgiltgpgDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEK-VRAVGQR 4705
Cdd:COG1196    302 QDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlLEAEAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4706 LSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDELKKRLETVALPLQGLEDLAADRI 4785
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEELEEALAELEEEEEEEEEALEEAAE 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4786 NRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVP 4865
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4866 PGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQKYQWHVEDLVpwiedckakMSEL 4929
Cdd:COG1196    530 IGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGA---------IGAA 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4930 RVTLDPVQLESSLLRSKAMLNEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMT 5009
Cdd:COG1196    601 VDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5010 QRLREFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQL 5089
Cdd:COG1196    679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
                          570
                   ....*....|....*..
gi 2020023496 5090 LHQAEVAQQEFLEVKQR 5106
Cdd:COG1196    759 PPDLEELERELERLERE 775
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
209-287 7.62e-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: 42.29  E-value: 7.62e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496  209 IKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSS 287
Cdd:cd21185     17 VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
4645-5388 9.16e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.26  E-value: 9.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4645 DVSLSTSQVQKELQSINQKWV-ELT-------DKLNSRSSQIDQAIVKSTQYQELLQD----LSEKVRAVGQRLSVQSAI 4712
Cdd:pfam15921  131 DIRRRESQSQEDLRNQLQNTVhELEaakclkeDMLEDSNTQIEQLRKMMLSHEGVLQEirsiLVDFEEASGKKIYEHDSM 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4713 STQPEAvkqqlEETSEIRSDLEQLDHEVkeaqtlcdelsvligeQYLKDELkkrletvaLPLQG-LEDLAADRINRLQAA 4791
Cdd:pfam15921  211 STMHFR-----SLGSAISKILRELDTEI----------------SYLKGRI--------FPVEDqLEALKSESQNKIELL 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4792 LASTQ-QFQQMFDELR---TWLDDKQSQ-QAKNCPISAKLERLQSQLQEN---------------EEFQKSLNQHSGSYE 4851
Cdd:pfam15921  262 LQQHQdRIEQLISEHEveiTGLTEKASSaRSQANSIQSQLEIIQEQARNQnsmymrqlsdlestvSQLRSELREAKRMYE 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4852 VIVAEGE-SLLLSVPPGEEKRTLQNQLV-ELKNHWEELSKKTADRQSRLKD-CMQKAQKYQWhvedlvpWIEDCKAKMS- 4927
Cdd:pfam15921  342 DKIEELEkQLVLANSELTEARTERDQFSqESGNLDDQLQKLLADLHKREKElSLEKEQNKRL-------WDRDTGNSITi 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4928 -ELRVTLDPVQLESSLLRS--KAMLNEVEKR--RSLLEILNSaadiliNSSEADEDGIRDEKAGINQNMDAVTEELQAKT 5002
Cdd:pfam15921  415 dHLRRELDDRNMEVQRLEAllKAMKSECQGQmeRQMAAIQGK------NESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5003 GSLEEMTQRLREFQESFKNIEKKVEGakhqleifdalgsqacSNKNLEKLRAQQEV----LQALEPQVDYLRNftqglve 5078
Cdd:pfam15921  489 MTLESSERTVSDLTASLQEKERAIEA----------------TNAEITKLRSRVDLklqeLQHLKNEGDHLRN------- 545
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5079 dAPDGSDASQLlHQAEvaQQEFLEVKQRvnsgcvMMENKLEGIGQfHCRVremfsqladlddeldgMGAIGRDTDSLQSQ 5158
Cdd:pfam15921  546 -VQTECEALKL-QMAE--KDKVIEILRQ------QIENMTQLVGQ-HGRT----------------AGAMQVEKAQLEKE 598
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5159 IEDVRLFLNKIHVLKldiEASEAECRHMLEEEGTLDLlglkRELEALNKQCGKLTERGKARQEQLELtLGRVEDFYRKLK 5238
Cdd:pfam15921  599 INDRRLELQEFKILK---DKKDAKIRELEARVSDLEL----EKVKLVNAGSERLRAVKDIKQERDQL-LNEVKTSRNELN 670
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5239 GLNDATTAAEEAEALQwvvGTEVEIINQQLadfkmfqKEQVDPLQMKLQQVNGLGQGLIQSAGKDCDVQ-GLEHDMEEIN 5317
Cdd:pfam15921  671 SLSEDYEVLKRNFRNK---SEEMETTTNKL-------KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmGMQKQITAKR 740
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 5318 ARWNTLNKKvaqrIAQLQEALLHCGKFQDALEPLLSWLADTEELIANQKPPSA-EYKVVKAqiQEQKLLQRL 5388
Cdd:pfam15921  741 GQIDALQSK----IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgELEVLRS--QERRLKEKV 806
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
5856-6288 9.24e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5856 EKTESLIQQYEAiSLLNSERYARLERAQVLVNQfwETYEELSPWIEETRALIAQLPSPA-IDHEQLRQQQEEMRQLRESI 5934
Cdd:pfam05483  222 EKIQHLEEEYKK-EINDKEKQVSLLLIQITEKE--NKMKDLTFLLEESRDKANQLEEKTkLQDENLKELIEKKDHLTKEL 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5935 AEHKPHIDKLLKIGPQLKE----------LNPEEGEMVEEKYQKAENMYAQIKEEVRQRALALDEAVSQSTQFHDKIEPM 6004
Cdd:pfam05483  299 EDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6005 LE----TLENLSSRLR-MPPLI---PAEVDKIRECISDNKSATVELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQ 6076
Cdd:pfam05483  379 LKiitmELQKKSSELEeMTKFKnnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6077 ---DKLDQMVFFWE--DIKARAEEREIKFLDVLELAEKFWYDMAALlttIKDTQDIVHDLESPGIDPSIIKQQVE----A 6147
Cdd:pfam05483  459 ltaIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQEDIINCKKQEErmlkQ 535
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6148 AETIKEETDGLHEELEFIR---ILGADLIfACGETEKPEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQ 6224
Cdd:pfam05483  536 IENLEEKEMNLRDELESVReefIQKGDEV-KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 6225 AmfdwlDNTVIKLCTMPPvGTDLNTVKDQLNEMkEFKVEVYQQQIEMEKLNHQGELMLKKATDE 6288
Cdd:pfam05483  615 Q-----ENKALKKKGSAE-NKQLNAYEIKVNKL-ELELASAKQKFEEIIDNYQKEIEDKKISEE 671
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5605-6123 9.31e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 9.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5605 EEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYADItvtsSKALRTLEQARQLATKFQSTYEELTGWLRE 5684
Cdd:PRK03918   182 EKFIKRTENIEELIKEKEKELEEVL-REINEISSELPELREELEKL----EKEVKELEELKEEIEELEKELESLEGSKRK 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5685 VEEELatsggqSPTGEQIPQFQQRQKELKKEVME--------------HRLVLDTVNEVSRALLELVPWRAR-EGLDKLV 5749
Cdd:PRK03918   257 LEEKI------RELEERIEELKKEIEELEEKVKElkelkekaeeyiklSEFYEEYLDELREIEKRLSRLEEEiNGIEERI 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5750 SDANEQYKLVSDTIGQRV---DEIDAAIQRSQQYEQAAdAELAWVAETKRKLMALGPIRLE---QDQTTAQLQVQKAFS- 5822
Cdd:PRK03918   331 KELEEKEERLEELKKKLKeleKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEkelEELEKAKEEIEEEISk 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5823 ---------IDIIRHKDSMDELFSHRSEIfGTCG-----EEQKTVLQEKTESLIQQYEAISLLnSERYARLERAQVLVNQ 5888
Cdd:PRK03918   410 itarigelkKEIKELKKAIEELKKAKGKC-PVCGrelteEHRKELLEEYTAELKRIEKELKEI-EEKERKLRKELRELEK 487
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5889 FWETYEELSPW---IEETRALIAQLPSpaIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEgEMVEEK 5965
Cdd:PRK03918   488 VLKKESELIKLkelAEQLKELEEKLKK--YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKK 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5966 YQKAENMYAQIKEEVRQRALA----LDEAVSQSTQFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNK----S 6037
Cdd:PRK03918   565 LDELEEELAELLKELEELGFEsveeLEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEkrleE 644
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 6038 ATVELEKLQPSF-----EALKRRGEELIGRSQGADKDLaaKEIQDKLDQMVFFWEDIKARAEEREiKFLDVLELAEKFWY 6112
Cdd:PRK03918   645 LRKELEELEKKYseeeyEELREEYLELSRELAGLRAEL--EELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALE 721
                          570
                   ....*....|.
gi 2020023496 6113 DMAALLTTIKD 6123
Cdd:PRK03918   722 RVEELREKVKK 732
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2363-2401 9.55e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.00  E-value: 9.55e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2020023496 2363 VLMADKAISGVLDPRTQTLCSVKDAVTVGLLDKETATRI 2401
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5452-5554 1.06e-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: 41.92  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5452 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLtSPAEQGVLSEKI 5531
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 2020023496 5532 DSLQARYSEIQDRCCRKAALLDQ 5554
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
4537-5348 1.07e-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: 46.19  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4537 QEAENWKKIQEELNSRWERATEVTVARQRQLEESASHLACFQAAESQLRPWLMEKELMMGVLGPLSIDPNMLNAQKQQVQ 4616
Cdd:TIGR00606  203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQME 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4617 FMLKEFEARRQQ-----HEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVEltdkLNSRSSQIDQAIVKSTQYQEL 4691
Cdd:TIGR00606  283 KDNSELELKMEKvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL----LNQEKTELLVEQGRLQLQADR 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4692 LQDLSEKVRAVGQRLSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDEL-SVLIGEQYLKDELKKRLETV 4770
Cdd:TIGR00606  359 HQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLqSKERLKQEQADEIRDEKKGL 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4771 ALPLQGLEDLAADRINRL-------QAALASTQQFQQMFDELRTWLDDkQSQQAKNCPISAKLERLQSQLQENEEFQKSL 4843
Cdd:TIGR00606  439 GRTIELKKEILEKKQEELkfvikelQQLEGSSDRILELDQELRKAERE-LSKAEKNSLTETLKKEVKSLQNEKADLDRKL 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4844 NQHSGSYEVIVAEGESLLLSVPPGEEKRTLQNQLVELK-NHWEELS-----------------------KKTADRQSRLK 4899
Cdd:TIGR00606  518 RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTsllgyfpnkkqledwlhskskeiNQTRDRLAKLN 597
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4900 DCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ-LESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADED 4978
Cdd:TIGR00606  598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4979 GIrdekAGINQNMDAVTEELQAKTGSLEEMTqrlREFQESFKNIEKKVEGAKHQLEIFdalgsqacsnknLEKLRAQQEV 5058
Cdd:TIGR00606  678 SC----CPVCQRVFQTEAELQEFISDLQSKL---RLAPDKLKSTESELKKKEKRRDEM------------LGLAPGRQSI 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5059 LQALEPQVDYLRNFTQGLVED-APDGSDASQLLHQAEVAQQEfLEVKQRVNSGCVMMEnklegigQFHCRVREMFSQLAD 5137
Cdd:TIGR00606  739 IDLKEKEIPELRNKLQKVNRDiQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIME-------RFQMELKDVERKIAQ 810
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5138 LDDELDGMGaIGRDTDSLQSQIEDvrlflnKIHvlKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNK---QCGKLTE 5214
Cdd:TIGR00606  811 QAAKLQGSD-LDRTVQQVNQEKQE------KQH--ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQ 881
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5215 RGKARQEQLELTLGRVEDFYRKLKglNDATTAAEEAEALQWVVGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQ 5294
Cdd:TIGR00606  882 RRQQFEEQLVELSTEVQSLIREIK--DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-VNDIKEKVKNIHGYMK 958
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2020023496 5295 GLIQSAGKDCDVQGLEHDMEeinarwntlnkkVAQRIAQLQEALLHCGKFQDAL 5348
Cdd:TIGR00606  959 DIENKIQDGKDDYLKQKETE------------LNTVNAQLEECEKHQEKINEDM 1000
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4708-5241 1.09e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4708 VQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQylkDELKKRLETVALPLQGLEDlaadRINR 4787
Cdd:PRK03918   191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI---EELEKELESLEGSKRKLEE----KIRE 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4788 LQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLllsvppG 4867
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK------E 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4868 EEKRTLQNQLVELKNHWEELsKKTADRQSRLKDCMQKAQKYQWHVEDLVPwiEDCKAKMSELRVTLDPVQLESSLLRSK- 4946
Cdd:PRK03918   338 ERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARi 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4947 -AMLNEVEKRRSLLEILNSAADIL-INSSEADEDgirdEKAGInqnMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEK 5024
Cdd:PRK03918   415 gELKKEIKELKKAIEELKKAKGKCpVCGRELTEE----HRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5025 KVEGAKH---QLEIFDALGS--QACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDapdgsdasqllhqaevaqqe 5099
Cdd:PRK03918   488 VLKKESElikLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-------------------- 547
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5100 fLEVKQRVNSGCVMMENKLegigqfhcrvREMFSQLADLDDELDGMGAigRDTDSLQSQIEDVRLFLNKIhvlkldieas 5179
Cdd:PRK03918   548 -LEKLEELKKKLAELEKKL----------DELEEELAELLKELEELGF--ESVEELEERLKELEPFYNEY---------- 604
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 5180 eaecrhmleeegtLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLN 5241
Cdd:PRK03918   605 -------------LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
SPEC smart00150
Spectrin repeats;
4906-5006 1.12e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  4906 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 4985
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 2020023496  4986 GINQNMDAVTEELQAKTGSLE 5006
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
4498-4835 1.13e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.10  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4498 VKAQAESNKAFLAELEQNSPKIQKVKEALAgllvtypnSQEA-ENWKKIQEELNSRWERATEVTVARQRQLEESASHLac 4576
Cdd:COG3096    315 LEELSARESDLEQDYQAASDHLNLVQTALR--------QQEKiERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL-- 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4577 fQAAESQLrpwlmeKELMMGVlgplsidpnmlnAQKQQVqfmLKEFEARRQQHEQLNEA---AQGILTGPgdvSLSTSQV 4653
Cdd:COG3096    385 -EAAEEEV------DSLKSQL------------ADYQQA---LDVQQTRAIQYQQAVQAlekARALCGLP---DLTPENA 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4654 QKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQ------------DLSEKVRAVGQRLSVQSAISTQPEAVKQ 4721
Cdd:COG3096    440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQRLQQLRA 519
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4722 QLeetseirSDLEQLDHEVKEAQTLCDELSVLIGEQY-LKDELKKRLETVALPLQGLEDLAADRINRLQAALASTQQFQQ 4800
Cdd:COG3096    520 QL-------AELEQRLRQQQNAERLLEEFCQRIGQQLdAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2020023496 4801 MFDELRT----WLDdkqSQQAkncpisakLERLQSQLQE 4835
Cdd:COG3096    593 RIKELAArapaWLA---AQDA--------LERLREQSGE 620
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4676-4897 1.19e-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: 45.53  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4676 SQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSVQSAISTQPEAVKQQLEET----SEIRSDLEQLDHEVKEAQTLCDELS 4751
Cdd:COG4942     17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarriRALEQELAALEAELAELEKEIAELR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4752 VLIGEQylKDELKKRLetVALPLQGLED-----LAADRINRLQAALASTQQF-QQMFDELRTWLDDKQSQQAKNCPISAK 4825
Cdd:COG4942     97 AELEAQ--KEELAELL--RALYRLGRQPplallLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALRAELEAE 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 4826 LERLQSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPpgEEKRTLQNQLVELKNHWEELSKKTADRQSR 4897
Cdd:COG4942    173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLEAEAAAAAER 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4355-4838 1.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4355 KELEKQIEHLKSLLDDWAskgTLVEEINCKGTSLENLIMEITAPDSQgktgsilpsvgssvgsvngyhtcKDLTEIQCDM 4434
Cdd:COG4717     74 KELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAELEELREE-----------------------LEKLEKLLQL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4435 SDVNLKYEKLGGVLHERQESLQAILNRMEEVH---KEANSVLQWLESKEEVLKSMDAMSSPTKTETVKAQAESNKAFLAE 4511
Cdd:COG4717    128 LPLYQELEALEAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4512 LEQNSPKIQKVKEALAGLLvtypnsqeaenwKKIQEELNSRWERATEVTVARQRQLEESASHLACFQAAE-SQLRPWLME 4590
Cdd:COG4717    208 LAELEEELEEAQEELEELE------------EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGgSLLSLILTI 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4591 KELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPG-DVSLSTSQVQKELQSInQKWVELTD 4669
Cdd:COG4717    276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRI-EELQELLR 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4670 KLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQRLsvqsaisTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQtlcde 4749
Cdd:COG4717    355 EAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL-------EQAEEYQELKEELEELEEQLEELLGELEELL----- 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4750 lsvligEQYLKDELKKRLETvalpLQGLEDLAADRINRLQAALASTQQfqqmfdELRTWLDDKQSQQAKncpisAKLERL 4829
Cdd:COG4717    423 ------EALDEEELEEELEE----LEEELEELEEELEELREELAELEA------ELEQLEEDGELAELL-----QELEEL 481

                   ....*....
gi 2020023496 4830 QSQLQENEE 4838
Cdd:COG4717    482 KAELRELAE 490
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2576-2607 1.44e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 39.62  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2020023496 2576 EVQAFTGNFVDLISGQRLTLAEAKKEGLLTNE 2607
Cdd:pfam00681    3 EAQAATGGIIDPVTGERLSVEEAVKRGLIDPE 34
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
4610-5166 1.47e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4610 AQKQQVQFMLKEFEARRQQHEQLNEAAqgiltgpgDVSLSTSQVQKELQSINQ----KWVELTDKLNSRSSQIDQAIVKS 4685
Cdd:pfam15921  294 ANSIQSQLEIIQEQARNQNSMYMRQLS--------DLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTER 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4686 TQYQELLQDLSEKVRAVGQRL-SVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIgeQYLKDELK 4764
Cdd:pfam15921  366 DQFSQESGNLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL--KAMKSECQ 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4765 KRLETVALPLQGlEDLAADRINRLQAALASTQQ-FQQMFDEL-----------RTWLDDKQSQQAKNCPISA---KLERL 4829
Cdd:pfam15921  444 GQMERQMAAIQG-KNESLEKVSSLTAQLESTKEmLRKVVEELtakkmtlesseRTVSDLTASLQEKERAIEAtnaEITKL 522
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4830 QSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVppgeekrTLQNQLVELKNHWEELSKKTADRQSRLKDCMQkAQKYQ 4909
Cdd:pfam15921  523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQM-------AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ-VEKAQ 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4910 WHVEdlvpwIEDCKAKMSELRVTLDpvqlessllRSKAMLNEVEKRRSLLEILNSAadiLINSSEADEDGIRDekagINQ 4989
Cdd:pfam15921  595 LEKE-----INDRRLELQEFKILKD---------KKDAKIRELEARVSDLELEKVK---LVNAGSERLRAVKD----IKQ 653
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4990 NMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEI------------FDALGSQACSNKNLEKLR-AQQ 5056
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqlksaqseleqtRNTLKSMEGSDGHAMKVAmGMQ 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5057 EVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVA-QQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQL 5135
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANM 809
                          570       580       590
                   ....*....|....*....|....*....|.
gi 2020023496 5136 ADLDDELDGMGAIGRDTDSLQSQiEDVRLFL 5166
Cdd:pfam15921  810 EVALDKASLQFAECQDIIQRQEQ-ESVRLKL 839
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
3564-3749 1.47e-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: 44.15  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3564 RQMLRLLNELQRsFQDILEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTQ-Q 3642
Cdd:COG1579      3 PEDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3643 DLSALQKNQSDLKDLQDDIQNRATSFATVVKDIEGFMEEnqtklspreLTALREKLHQAKEQYEALQEETRVAQKELEEA 3722
Cdd:COG1579     80 EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER---------IEELEEELAELEAELAELEAELEEKKAELDEE 150
                          170       180
                   ....*....|....*....|....*..
gi 2020023496 3723 VTSALQQETEKSKAAKELAenkKKIDA 3749
Cdd:COG1579    151 LAELEAELEELEAEREELA---AKIPP 174
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
7379-7553 1.55e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7379 PSSPATPASGTKTSLQFSRC-YDKPWLVNSKAGTP-------IRDSHSPDLQLPTPEViPSSGSKLKRPTPTFHSSRTSL 7450
Cdd:PHA03307    84 SRSTPTWSLSTLAPASPAREgSPTPPGPSSPDPPPptpppasPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPAAV 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7451 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLL-ETQSACSD 7513
Cdd:PHA03307   163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGaSSSDSSSS 242
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2020023496 7514 TSESSAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 7553
Cdd:PHA03307   243 ESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3552-3758 1.78e-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: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3552 SEHAQDLSPQ-QNRQMLRLLNELQRSFqdILE--QTAAQVDALQGHLQQMEQ-EALVKTLQKQQNTchqqLEDLcswVGQ 3627
Cdd:COG4913    190 SEKALRLLHKtQSFKPIGDLDDFVREY--MLEepDTFEAADALVEHFDDLERaHEALEDAREQIEL----LEPI---REL 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3628 AERALAGHQGRTTQQDLSA---LQKNQSDLKDLQDDIQNRAtsfatvvkdiegfmeenqtklspRELTALREKLHQAKEQ 3704
Cdd:COG4913    261 AERYAAARERLAELEYLRAalrLWFAQRRLELLEAELEELR-----------------------AELARLEAELERLEAR 317
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 3705 YEALQEETRVAQKELEEAVTSALQQ-ETEKSKAAKELAENKKKIDALLDWVTSVG 3758
Cdd:COG4913    318 LDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALG 372
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
4650-5027 1.84e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4650 TSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSVQSA----ISTQPEAVKQQLEE 4725
Cdd:TIGR04523  227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4726 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRINRLQAALASTQQFQQMFD 4803
Cdd:TIGR04523  307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4804 ELRTWLDDKQS--QQAKNCPIS-AKLER-LQSQLQENEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 4878
Cdd:TIGR04523  371 EIEKLKKENQSykQEIKNLESQiNDLESkIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4879 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLNE 4951
Cdd:TIGR04523  451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 4952 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVE 5027
Cdd:TIGR04523  531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
7151-7208 1.92e-03

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


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 44.19  E-value: 1.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 7151 FRRIDKDQDGKITRQEFIDGILASKFPTTK-LEMTAVADIFDRDGDGYIDYYEFVAALH 7208
Cdd:cd16230    129 FRVADQDGDSMATREELTAFLHPEEFPHMRdIVVAETLEDLDKNKDGYVQVEEYIADLY 187
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4654-4894 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4654 QKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAvgqrLSVQSAISTQpEAVKQQLEETSeirSDL 4733
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----ASAEREIAEL-EAELERLDASS---DDL 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4734 EQLDHEVKEAQTLCDELSVLIGEQYLK-DELKKRLETVALPLQGLEDLAADRINRLQAALAstQQFQQMFDELRtwLDDK 4812
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEiGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAAL--GDAV 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4813 QSQQAKNcpISAKLERLQSQL-QENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKRT-LQNQ-LVELKNHWEELSK 4889
Cdd:COG4913    764 ERELREN--LEERIDALRARLnRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDrLEEDgLPEYEERFKELLN 841

                   ....*
gi 2020023496 4890 KTADR 4894
Cdd:COG4913    842 ENSIE 846
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
3681-3905 2.15e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3681 ENQTKLSPRELTALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLD----WVTS 3756
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgeRARA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3757 VGSSGGqlltNLPGMEQLSGAsleKGALDTTDGYMGVNQapekldkqcemmkarhqeLLSQQQNFILATQSAQAFLDqhg 3836
Cdd:COG3883     95 LYRSGG----SVSYLDVLLGS---ESFSDFLDRLSALSK------------------IADADADLLEELKADKAELE--- 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020023496 3837 hnltpEEQQMLQQKLGELKEQystsLAQSEAELKQVQTLQDELQKFLQDHKEFESWLERSEKELENMHK 3905
Cdd:COG3883    147 -----AKKAELEAKLAELEAL----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3400-3899 2.15e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3400 LLCQAKVLERELKDLTTLVSQELECVNQiiISQPQEVPAQLLKALEKDAKNLQKSLSSVSDTWNsRLLHFQNAVEIE--- 3476
Cdd:pfam05483  245 LLIQITEKENKMKDLTFLLEESRDKANQ--LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-RSMSTQKALEEDlqi 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3477 KTKVLNQHT-QLEGRLQDLRAWVGNKNLILnskgSNSEIDVDSLNLCLQQYEdlkQPMAERKAQLDALAFDIQFFISEHA 3555
Cdd:pfam05483  322 ATKTICQLTeEKEAQMEELNKAKAAHSFVV----TEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3556 QDLSPQQNRQM-LRLLNELQRSFQDILEQTaAQVDALQGHLQQMEQEaLVKTLQKQQNTCH-----------------QQ 3617
Cdd:pfam05483  395 EMTKFKNNKEVeLEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQE-LIFLLQAREKEIHdleiqltaiktseehylKE 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3618 LEDLCSWVGQAE---RALAGHQGRTTQQDLSALQKNQS---DLKDLQDDIQNRATSFATVVKDIEGfMEENQTKLSpREL 3691
Cdd:pfam05483  473 VEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLR-DEL 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3692 TALREKLHQAKEQ----YEALQEETRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLLTN 3767
Cdd:pfam05483  551 ESVREEFIQKGDEvkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3768 LPGME------QLSGASLEKGALDTTDGYMGVNQ----APEKLDKQCEMMKARHQELLSQQQNFILATQ----SAQAFLD 3833
Cdd:pfam05483  631 LNAYEikvnklELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaEMVALME 710
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 3834 QHGHnltpEEQQMLQQKLGEL-----KEQYSTSLAQS-EAELKQVQTLQDELQKFLQDHKEFESWLERSEKE 3899
Cdd:pfam05483  711 KHKH----QYDKIIEERDSELglyknKEQEQSSAKAAlEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
4054-4367 2.24e-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: 45.04  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4054 EKLQKVARDIMEIEGEPAPDHRHVQETTDSILS-------HFQSlSYSLAERSSLLQKAIAQSQSVQESLESLLQSIGEV 4126
Cdd:TIGR00606  646 EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQT-EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4127 EQNLEGK---QVSSLSSGV--IQEALATNMKLKQDIARQKSSLEATREMVTRFMetADSTTAAVLQGKLAeVSQRFeqlc 4201
Cdd:TIGR00606  725 RDEMLGLapgRQSIIDLKEkeIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM--PEEESAKVCLTDVT-IMERF---- 797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4202 lqQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRmlasgNQPDQDITHFFQQIQELNLEMEDQQENLDTLEHLVTELS 4281
Cdd:TIGR00606  798 --QMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-----QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4282 ScgFALDLCQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQ---LDEFRKLVRTFQKWL---KETEGSIPPTETSMSAK 4355
Cdd:TIGR00606  871 S--EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELissKETSNKKAQDKVNDIKE 948
                          330
                   ....*....|..
gi 2020023496 4356 ELEKQIEHLKSL 4367
Cdd:TIGR00606  949 KVKNIHGYMKDI 960
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
4164-5125 2.65e-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: 45.04  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4164 LEATREMVTRFMETADSTTAAVLQGKLAEVSQRFEQlclQQQEKESSLKKLLPQAEMFEHLSGKL--QQFMENKSRMLAS 4241
Cdd:TIGR00606  165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQ---KVQEHQMELKYLKQYKEKACEIRDQItsKEAQLESSREIVK 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4242 GNQPDQD--------ITHFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGFALdlcqHQDRVQNLRKDFTELQKTVKER 4313
Cdd:TIGR00606  242 SYENELDplknrlkeIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----FQGTDEQLNDLYHNHQRTVREK 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4314 EKDASSCQEQLDEFRKLVRTFQKwlKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTL--VEEINCKGTSLENL 4391
Cdd:TIGR00606  318 ERELVDCQRELEKLNKERRLLNQ--EKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgFERGPFSERQIKNF 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4392 I-MEITAPDSQGKTGSILPSVGSSvgsvNGYHTCKDLTEIQCDMSDVNLKYEKLGGVLHERQESLQAILNRMEEVHKEAN 4470
Cdd:TIGR00606  396 HtLVIERQEDEAKTAAQLCADLQS----KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4471 SVLQWLESKEEVLKSMDAMSSPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALagllvtypnSQEAENWKKIQEELN 4550
Cdd:TIGR00606  472 RILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL---------NHHTTTRTQMEMLTK 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4551 SRWERATEVTVARQRQLEESASHLACFqAAESQLRPWLM----EKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARR 4626
Cdd:TIGR00606  543 DKMDKDEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHskskEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4627 QQHEQ-LNEAAqgiltGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQdlsekvRAVGQR 4705
Cdd:TIGR00606  622 SSYEDkLFDVC-----GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ------RVFQTE 690
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4706 LSVQsaistqpEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLI-GEQYLKDELKKRLETVAlplqgledlaadr 4784
Cdd:TIGR00606  691 AELQ-------EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApGRQSIIDLKEKEIPELR------------- 750
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4785 iNRLQAALASTQQFQQMFDELRTWLD--DKQSQQAKNCPISAK-LERLQSQLQENEEfqkslnqhsgSYEVIVAEGESll 4861
Cdd:TIGR00606  751 -NKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTiMERFQMELKDVER----------KIAQQAAKLQG-- 817
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4862 lsvppgeekrtlqnqlVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVtlDPVQLESS 4941
Cdd:TIGR00606  818 ----------------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS--EKLQIGTN 879
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4942 LLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKN 5021
Cdd:TIGR00606  880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5022 IEKKV-EGAKHQL-----EIFDALGSQACSNKNLEK----LRAQQEVLQALEPQVDYLR-NFTQGLVEDAPDGSDASQLL 5090
Cdd:TIGR00606  960 IENKIqDGKDDYLkqketELNTVNAQLEECEKHQEKinedMRLMRQDIDTQKIQERWLQdNLTLRKRENELKEVEEELKQ 1039
                          970       980       990
                   ....*....|....*....|....*....|....*
gi 2020023496 5091 HQAEVAQQEFLEVKQRVNSgcvmMENKLEGIGQFH 5125
Cdd:TIGR00606 1040 HLKEMGQMQVLQMKQEHQK----LEENIDLIKRNH 1070
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
4621-5037 2.75e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4621 EFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKEL--------QSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELL 4692
Cdd:pfam05483  177 EREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhfklkedhEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4693 QDLS---EKVRAVGQRLSVQSAIstQPEAVKQQLEETSEIRSDLE----QLDHEVKEAQTLCDELSVLIGEQYlkdELKK 4765
Cdd:pfam05483  257 KDLTfllEESRDKANQLEEKTKL--QDENLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKTIC---QLTE 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4766 RLETVALPLQGLEDLAADRINRLQAALASTQQFqqmfdeLRTWLDDKQSQQAKNCPISAKLERLQSQLQENEEFQKSLNQ 4845
Cdd:pfam05483  332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4846 HSGSYEVIVAEGESLLlsvppgEEKRTLQNQLVELKNHWEELS-------KKTADRQSRLKDCMQKAQKYQWHVEDLVPW 4918
Cdd:pfam05483  406 ELEELKKILAEDEKLL------DEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4919 IEDCKAKMSELRVTLDPVQLESSLLRSKA-----------------------MLNEVE----KRRSLLEILNSAADILI- 4970
Cdd:pfam05483  480 LEKEKLKNIELTAHCDKLLLENKELTQEAsdmtlelkkhqediinckkqeerMLKQIEnleeKEMNLRDELESVREEFIq 559
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020023496 4971 ---------NSSEADEDGIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEIFD 5037
Cdd:pfam05483  560 kgdevkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
SPEC smart00150
Spectrin repeats;
3615-3720 2.85e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 2.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496  3615 HQQLEDLCSWVGQAERALAGHQgrtTQQDLSALQKNQSDLKDLQDDIQNRATSFATVVKDIEGFMEENqtklsPRELTAL 3694
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 2020023496  3695 REKLHQAKEQYEALQEETRVAQKELE 3720
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
4676-4896 2.91e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4676 SQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSvqsAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSVLIG 4755
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4756 EQ----YLKDELKKRLETVAlplqGLEDLaADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLQS 4831
Cdd:COG3883     90 ERaralYRSGGSVSYLDVLL----GSESF-SDFLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKLAELEA 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 4832 QLQENEEFQKSLNQHSGSYEVIVAEGEslllsvppgEEKRTLQNQLVELKNHWEELSKKTADRQS 4896
Cdd:COG3883    162 LKAELEAAKAELEAQQAEQEALLAQLS---------AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4608-5019 3.04e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4608 LNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGpgdvslstSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQ 4687
Cdd:COG4717    100 LEEELEELEAELEELREELEKLEKLLQLLPLYQEL--------EALEAELAELPERLEELEERLEELRELEEELEELEAE 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4688 YQELLQDLSEKVRAVgqRLSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKDELKK-- 4765
Cdd:COG4717    172 LAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEar 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4766 ---RLETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLQSQLQENEEFQKS 4842
Cdd:COG4717    250 lllLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4843 LN-----QHSGSYEVIVAEGESLLLSVPPGEEKRTLQNQLVELKNHWEELSKKTAD----RQSRLKDCMQKAQKYQWHVE 4913
Cdd:COG4717    330 LPpdlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELEELEE 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4914 DLvpwiEDCKAKMSELRVTLDPVQLESSLLRSKAMLNEVEKRRSllEILNSAADILINSSEADEDG----IRDEKAGINQ 4989
Cdd:COG4717    410 QL----EELLGELEELLEALDEEELEEELEELEEELEELEEELE--ELREELAELEAELEQLEEDGelaeLLQELEELKA 483
                          410       420       430
                   ....*....|....*....|....*....|
gi 2020023496 4990 NMDAVTEELQAKTGSLEEMTQRLREFQESF 5019
Cdd:COG4717    484 ELRELAEEWAALKLALELLEEAREEYREER 513
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
4687-5436 3.79e-03

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: 44.57  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4687 QYQELLQDLSEKVRAVGQRLSVQSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSvligeQYLKDELKKR 4766
Cdd:TIGR00618  202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA---YLTQKREAQEEQLKKQQLLK-----QLRARIEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4767 LETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLddkQSQQAKNCPISAKLERLQSQLQENEEFQKSLNQH 4846
Cdd:TIGR00618  274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL---QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4847 SGSYEVIVAEGEslllsvppgeekrtlqnqlvELKNHWEELSKKTADRQSRLKDCMQKAqkyqwHVEDLVPWIEDCKAKM 4926
Cdd:TIGR00618  351 HSQEIHIRDAHE--------------------VATSIREISCQQHTLTQHIHTLQQQKT-----TLTQKLQSLCKELDIL 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4927 SELRVTLDPVQLESSLLRSK--AMLNEVEKRRSLLEILNSAADILINSSEADEDGIR------DEKAGINQNMDAVTEEL 4998
Cdd:TIGR00618  406 QREQATIDTRTSAFRDLQGQlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQesaqslKEREQQLQTKEQIHLQE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4999 QAKTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEIFDALGSQACsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVE 5078
Cdd:TIGR00618  486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ--RGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5079 dapdgsdasqllhQAEVAQQEFLEVKQRVNSGCVMMENKLEgigqfhcrvremfsQLADLDDELDgmgaigrdtdsLQSQ 5158
Cdd:TIGR00618  564 -------------QMQEIQQSFSILTQCDNRSKEDIPNLQN--------------ITVRLQDLTE-----------KLSE 605
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5159 IEDVRLFLNKIHVLKLDIEASEAECRHML---EEEGTLDLLGLKRELEALNKQcgKLTERGKARQEQLELTLGRVEDFYR 5235
Cdd:TIGR00618  606 AEDMLACEQHALLRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQE--RVREHALSIRVLPKELLASRQLALQ 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5236 KLKglNDATTAAEEAEALQWVVGTEVEIINQQLADFKMFQKEQ--VDPLQMKLQQVNGLGQGLIQSAGKDCDVQgLEHdM 5313
Cdd:TIGR00618  684 KMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnaSSSLGSDLAAREDALNQSLKELMHQARTV-LKA-R 759
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5314 EEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLADTEELIaNQKPPSAEYKVVKAQIQEQKLLQRlLDDRK 5393
Cdd:TIGR00618  760 TEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI-GQEIPSDEDILNLQCETLVQEEEQ-FLSRL 837
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|...
gi 2020023496 5394 ATVDMLQAEGGRiaQSAELADREKITGQLESLESRWTELLSKA 5436
Cdd:TIGR00618  838 EEKSATLGEITH--QLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
mukB PRK04863
chromosome partition protein MukB;
4542-4845 4.01e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4542 WKKIQEELNSRWERATEVtvarQRQLEESASHLACFQAAESQLRPWLmekELMMgvlgplsidpNMLNAQKQ--QVQFML 4619
Cdd:PRK04863   295 LYTSRRQLAAEQYRLVEM----ARELAELNEAESDLEQDYQAASDHL---NLVQ----------TALRQQEKieRYQADL 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4620 KEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAI-----VKS--------- 4685
Cdd:PRK04863   358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVqalerAKQlcglpdlta 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4686 -------TQYQELLQDLSEKVRAVGQRLSVQSAISTQPEAVKQQL-------------EETSEIRSDLEQLDHEVKEAQT 4745
Cdd:PRK04863   438 dnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagevsrseawDVARELLRRLREQRHLAEQLQQ 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4746 LCDELSVLIGE-------QYLKDELKKRLETVALPLQGLEDLAADrinrLQAALASTQQFQQMFDELRTWLDDKQSQqak 4818
Cdd:PRK04863   518 LRMRLSELEQRlrqqqraERLLAEFCKRLGKNLDDEDELEQLQEE----LEARLESLSESVSEARERRMALRQQLEQ--- 590
                          330       340
                   ....*....|....*....|....*..
gi 2020023496 4819 ncpISAKLERLQSQLQENEEFQKSLNQ 4845
Cdd:PRK04863   591 ---LQARIQRLAARAPAWLAAQDALAR 614
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5257-5336 4.38e-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: 40.38  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5257 VGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQLQE 5336
Cdd:pfam00435   29 YGKDLESVQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
3525-3888 4.51e-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: 44.06  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3525 QYEDLKQPMAERKAQLDALAFDIQFFISEHAQDLSP-----QQNRQMLRLLNELQRSFQDI-LEQTAAQVDALQGHLQQM 3598
Cdd:pfam12128  277 RQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAadaavAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSEL 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3599 E-QEALVKTLQKQQNTCHQQLEDLCSWVG-QAERALAG-HQGRTTQQDLSALQKN--QSDLKDLQDDIQNRATSFATVVK 3673
Cdd:pfam12128  357 EnLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGiKDKLAKIREARDRQLAvaEDDLQALESELREQLEAGKLEFN 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3674 DIEGFMEE---------NQTKLSPRELT----------ALREKLHQAKEQYEALQEETRVAQKELEEAVTSALQQETEKS 3734
Cdd:pfam12128  437 EEEYRLKSrlgelklrlNQATATPELLLqlenfderieRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3735 KAAKELAENKKKIDA----LL--------DWVTSVGS--SGGQLL-TNL---------PGMEQLSGASLEKGALDTTDGY 3790
Cdd:pfam12128  517 ERQSALDELELQLFPqagtLLhflrkeapDWEQSIGKviSPELLHrTDLdpevwdgsvGGELNLYGVKLDLKRIDVPEWA 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3791 MGVNQAPEKLDKQCEMM---KARHQELLSQ--QQNFILATQSA----------QAFLDQhgHNLTPEEQQM---LQQKLG 3852
Cdd:pfam12128  597 ASEEELRERLDKAEEALqsaREKQAAAEEQlvQANGELEKASReetfartalkNARLDL--RRLFDEKQSEkdkKNKALA 674
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2020023496 3853 ELKEQYSTSLAQSEAELKQvqtLQDELQKFLQDHKE 3888
Cdd:pfam12128  675 ERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKE 707
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
5852-6109 4.69e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5852 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpspaidhEQLR 5921
Cdd:COG0497    116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5922 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYQKAENmYAQIKEEVRQRALALDE------ 5989
Cdd:COG0497    179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 5990 --------AVSQSTQFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 6051
Cdd:COG0497    244 dllgqalrALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 6052 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 6109
Cdd:COG0497    311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3523-3751 4.76e-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: 43.90  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3523 LQQYEDLKQPMAERKAQLDALAFDIQFFISEHAQDLSPQQNRqmLRLLNELQRSFQDILEQTAAQVDALQGHLQQMEQE- 3601
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEl 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3602 -ALVKTLQKQQNTCHQ---QLEDLcswvgqaERALAGHQGRTTQQDLSALQKNQS------------------------- 3652
Cdd:TIGR02169  761 kELEARIEELEEDLHKleeALNDL-------EARLSHSRIPEIQAELSKLEEEVSriearlreieqklnrltlekeylek 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 3653 ---DLKDLQDDIQNRATSFATVVKDIEGFMEENQTKLSPRE--LTALREKLHQAKEQYEALQEETRVAQK---ELEEAVT 3724
Cdd:TIGR02169  834 eiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaaLRDLESRLGDLKKERDELEAQLRELERkieELEAQIE 913
                          250       260
                   ....*....|....*....|....*..
gi 2020023496 3725 SALQQETEKSKAAKELAENKKKIDALL 3751
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPK 940
PLEC smart00250
Plectin repeat;
1807-1838 4.98e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 4.98e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2020023496  1807 QLQTGGIIDTVTGQRLTIDEAVSNDLVAAKIA 1838
Cdd:smart00250    7 QSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1850-1879 5.09e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 5.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2020023496 1850 GLLWPESGEILPITDALEQGIVSTELAHKI 1879
Cdd:pfam00681   10 GIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
4621-5070 5.12e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4621 EFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVKSTQYQELLQDLSEKV- 4699
Cdd:PRK02224   280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAe 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4700 RAVGQRLSVQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGE-QYLKDELKKRLETVALPLQGLE 4778
Cdd:PRK02224   360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElREERDELREREAELEATLRTAR 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4779 DlaadRINRLQAALA------------------STQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLQSQLQENEEFQ 4840
Cdd:PRK02224   440 E----RVEEAEALLEagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEE---VEERLERAEDLVEAEDRIE 512
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4841 KSLNQHSGSYEVIVAEGESLllsvppgEEKRTlqnQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDlvpwie 4920
Cdd:PRK02224   513 RLEERREDLEELIAERRETI-------EEKRE---RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE------ 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4921 dCKAKMSELRVTLDPVQ-LESSLLRSKAMLNEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINqnmDAVTEELQ 4999
Cdd:PRK02224   577 -LNSKLAELKERIESLErIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD---EARIEEAR 652
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020023496 5000 AK----TGSLEEMTQRLREFQESFKNIEKKVEGAKHQLEifdalgsqacsnkNLEKLRaqqEVLQALEPQVDYLR 5070
Cdd:PRK02224   653 EDkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------------ELEELR---ERREALENRVEALE 711
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1159-1338 5.42e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.05  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1159 RSIQDAELLVKGYEIKLSQEEVVlADLSALEAHWSTLRHWLSDVKDKNSVFSVLDEEiakakvvAEQMSRLTPERNLDLE 1238
Cdd:cd00176      7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 1239 RYQEkgsQLQERWHRVIAQLEIRQSELESIQEVLGDYRACHgTLIKWIEETTAQQEMMKPGQAEDSrvLSEQLSQQTALF 1318
Cdd:cd00176     79 ERLE---ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELE 152
                          170       180
                   ....*....|....*....|
gi 2020023496 1319 AEIERNQTKLDQCQKFSQQY 1338
Cdd:cd00176    153 EELEAHEPRLKSLNELAEEL 172
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
45-88 6.23e-03

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


Pssm-ID: 409153  Cd Length: 107  Bit Score: 39.99  E-value: 6.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2020023496   45 KTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLE 88
Cdd:cd21304      4 KVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLE 47
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
7379-7555 6.41e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7379 PSSPATPASGTKTSLQFSRCYDKPWLVNSKAGTPirdshspdlqLPTPEVIPSSgsklkRPTPTFHSSRTSLAGDTSNSS 7458
Cdd:PHA03307   225 GRSAADDAGASSSDSSSSESSGCGWGPENECPLP----------RPAPITLPTR-----IWEASGWNGPSSRPGPASSSS 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 7459 SPASTGAKTNRADPKKSASRPGSRAgsrAGSRASSRRGSDASDfdlletqSACSDTSESSAAG-GQGNSRRGLNKPSKIP 7537
Cdd:PHA03307   290 SPRERSPSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSST-------SSSSESSRGAAVSpGPSPSRSPSPSRPPPP 359
                          170
                   ....*....|....*...
gi 2020023496 7538 tmskkTTTASPRTPGPKR 7555
Cdd:PHA03307   360 -----ADPSSPRKRPRPS 372
PLEC smart00250
Plectin repeat;
2285-2317 6.82e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.85  E-value: 6.82e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2020023496  2285 LNVLSAQLLDGGIFHEQTGQKLLLNEAISRGIV 2317
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4610-4824 7.57e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 7.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4610 AQKQQVQFMLKEFEARRQQHEQLNEAAQgiltgpgDVSLSTSQVQKELQSINQKWVELTDKLNSRSSQIDQAIVK----S 4685
Cdd:COG4942     17 AQADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4686 TQYQELLQDLSEKVRAVGQRLSVQSAISTQPEA----------------------VKQQLEETSEIRSDLEQLDHEVKEA 4743
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAEL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4744 QTLCDELSVLIGEQylkDELKKRLETVALPLQGLEDLAADRINRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPIS 4823
Cdd:COG4942    170 EAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

                   .
gi 2020023496 4824 A 4824
Cdd:COG4942    247 G 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4669-5061 8.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4669 DKLNSRSSQIDQAIVKSTQYQELLQDLSEkvravgqrlsvqsaISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCD 4748
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEE--------------LEEELEELEAELEELREELEKLEKLLQLLPLYQELEA 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4749 ELSVLIGEQYLKDELKKRLETVALPLQGLEDLAADRI---NRLQAALAST-----QQFQQMFDELRTWLDDKQSQQAKNC 4820
Cdd:COG4717    137 LEAELAELPERLEELEERLEELRELEEELEELEAELAelqEELEELLEQLslateEELQDLAEELEELQQRLAELEEELE 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4821 PISAKLERLQSQLQENEEF------QKSLNQHSGSYE------VIVAEGESLLLSVPPGEEKRTLQNQLVELknHWEELS 4888
Cdd:COG4717    217 EAQEELEELEEELEQLENEleaaalEERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLA 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4889 KKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMS-ELRVTLDPVQLESSLLRSKAMLNEVEKRRSLLEILNSAAD 4967
Cdd:COG4717    295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4968 ILINSSEADEDGIR------DEKAGINQNMDAVTEELQAKTGSL---------EEMTQRLREFQESFKNIEKKVEGAKHQ 5032
Cdd:COG4717    375 LLAEAGVEDEEELRaaleqaEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEELEELREE 454
                          410       420
                   ....*....|....*....|....*....
gi 2020023496 5033 LEIFDALGSQACSNKNLEKLRAQQEVLQA 5061
Cdd:COG4717    455 LAELEAELEQLEEDGELAELLQELEELKA 483
mukB PRK04863
chromosome partition protein MukB;
4611-5061 9.21e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4611 QKQQVQFMLKEFEAR--------------RQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQ-------SINQKWVELTD 4669
Cdd:PRK04863   531 QQQRAERLLAEFCKRlgknlddedeleqlQEELEARLESLSESVSEARERRMALRQQLEQLQariqrlaARAPAWLAAQD 610
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4670 KLNSRSSQIDQAIVKSTQYQELLQDLSEKVRAVGQrlsVQSAISTQPEAVKQQLEETSEIR-SDLEQLdhevkeaQTLCD 4748
Cdd:PRK04863   611 ALARLREQSGEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLSQPGgSEDPRL-------NALAE 680
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4749 ELS-VLIGEQY----LKDE--------------LKKRLETVALPLQGLEDLAAD------RINRLQAALASTQQF----- 4798
Cdd:PRK04863   681 RFGgVLLSEIYddvsLEDApyfsalygparhaiVVPDLSDAAEQLAGLEDCPEDlyliegDPDSFDDSVFSVEELekavv 760
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4799 ------------------------QQMFDELRTWLDDKQSQQAKNCPISAKLERLqsqlqeNEEFQKSLNQHSgsyeviv 4854
Cdd:PRK04863   761 vkiadrqwrysrfpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRL------HQAFSRFIGSHL------- 827
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4855 aegeSLLLSVPPGEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWH--------VEDLVPWIEDCKAKM 4926
Cdd:PRK04863   828 ----AVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQL 903
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4927 SELRVT-------------LDPV------------QLESSLLRSKAMLNEVEKRRSLLEILNS---------AADILINS 4972
Cdd:PRK04863   904 DEAEEAkrfvqqhgnalaqLEPIvsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKN 983
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023496 4973 SEADEDgIRDEKAGINQNMDAVTEELQAKTGSLEEMTQRLREFQESFKNIEKKVEGAKHQLeifDALGSQACSNKnLEKL 5052
Cdd:PRK04863   984 SDLNEK-LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADSGA-EERA 1058

                   ....*....
gi 2020023496 5053 RAQQEVLQA 5061
Cdd:PRK04863  1059 RARRDELHA 1067
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7120-7171 9.29e-03

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.91  E-value: 9.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023496 7120 ELKE-FANFDFD----VWRKKYMRWMNH-----KKSRVMDFFRRIDKDQDGKITRQEFIDGI 7171
Cdd:cd00051      1 ELREaFRLFDKDgdgtISADELKAALKSlgeglSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
 
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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