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Conserved domains on  [gi|67782321|ref|NP_001020029|]
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spectrin beta chain, erythrocytic isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
25-156 7.72e-84

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: 270.77  E-value: 7.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   25 APDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPT 104
Cdd:cd21317    1 LADDDWDNDNSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  105 KGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21317   81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
170-281 1.54e-82

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: 266.10  E-value: 1.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  170 RETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIP 249
Cdd:cd21319    1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 67782321  250 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 281
Cdd:cd21319   81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
2181-2286 2.50e-55

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269975  Cd Length: 106  Bit Score: 187.82  E-value: 2.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2181 MEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLRL 2260
Cdd:cd10571    1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321 2261 SNGSEWLFHGKDEEEMLSWLQGVSTA 2286
Cdd:cd10571   81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-742 5.22e-35

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 134.11  E-value: 5.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  530 LQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKgyqPCDPQVIQ 609
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG---HPDAEEIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  610 DRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGL 689
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321  690 DAHLEQIFQEAHGMVARKQFGH-PQIEARIKEVSAQWDQLKDLAAFCKKNLQDA 742
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1485-1690 7.68e-34

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 130.64  E-value: 7.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1485 RDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQS 1564
Cdd:cd00176    7 RDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1565 SWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLA 1644
Cdd:cd00176   87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLN 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 67782321 1645 SRAQGLLSAGHPEGEQIIRLQ-GQVDKHYAGLKDVAEERKRKLENMY 1690
Cdd:cd00176  167 ELAEELLEEGHPDADEEIEEKlEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-848 5.53e-32

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 125.25  E-value: 5.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  641 KFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKE 720
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  721 VSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVME 800
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321  801 HLEQQAQGFPEE--FRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEAL 848
Cdd:cd00176  164 SLNELAEELLEEghPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
955-1168 8.28e-32

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated 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: 8.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  955 RVHNYCVDCEETSKWITDKTKVVESTkDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQ 1034
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1035 RQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQ 1114
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321 1115 DSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCL 1168
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
745-954 1.30e-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: 124.10  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  745 FFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFR-DSPDVTHRL 823
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  824 QALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQ 903
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  904 IDGVNLAANSLVESGHP-RSREVKQYQDHLNTRWQAFQTLVSERREAVDSAL 954
Cdd:cd00176  162 LKSLNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1798-2005 2.98e-28

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 114.47  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1798 DLHRYFYTGAEILGLIDEKHRELP-EDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEkAEAIQN 1876
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1877 KEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRS 1956
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321 1957 KNFSACLELGESLLQRQHQAS-EEIREKLQQVMSRRKEMNEKWEARWERL 2005
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1170-1379 3.24e-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: 111.38  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1170 FQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKV 1249
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1250 QLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEG 1327
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKeaALASEDLGKDLE-SVEELLKKHKELEEELEAHEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 67782321 1328 WLENIDAEGKQLMDEKPQF-TALVSQKLEALHRLWDELQATTKEKTQHLSAAR 1379
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1691-1901 1.29e-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: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1691 HLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIAE 1770
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAH-EERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1771 WKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHREL-PEDVGLDASTAESFHRVHTAFERELHLLG 1849
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALaSEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321 1850 VQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVD 1901
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
422-525 1.69e-19

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: 85.45  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    422 QLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITA 501
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 67782321    502 RKDNILRLWSYLQELLQSRRQRLE 525
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
1385-1475 2.58e-08

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 2.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1385 LQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEK------ 1458
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEErleeln 83
                            90
                    ....*....|....*...
gi 67782321    1459 -RFLDLLEPLGRRKKQLE 1475
Cdd:smart00150   84 eRWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2013-2070 3.94e-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: 53.09  E-value: 3.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321   2013 QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEK 2070
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
302-412 4.26e-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: 53.09  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    302 KMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAfstYRTVEKPPKFQEkGNLEVLlfTIQSRMRANNQKVY 381
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELAAHQ-DRVEAL--NELAEKLIDEGHYA 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 67782321    382 TPHDGKLVSDINRAWESLEEAEYRRELALRN 412
Cdd:pfam00435   75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
25-156 7.72e-84

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: 270.77  E-value: 7.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   25 APDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPT 104
Cdd:cd21317    1 LADDDWDNDNSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  105 KGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21317   81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
170-281 1.54e-82

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: 266.10  E-value: 1.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  170 RETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIP 249
Cdd:cd21319    1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 67782321  250 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 281
Cdd:cd21319   81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
2181-2286 2.50e-55

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 187.82  E-value: 2.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2181 MEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLRL 2260
Cdd:cd10571    1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321 2261 SNGSEWLFHGKDEEEMLSWLQGVSTA 2286
Cdd:cd10571   81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
48-438 3.82e-54

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 201.71  E-value: 3.82e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   48 LADEREVVQKKTFTKWVNSHLARVSC-RITDLYKDLRDGRMLIKLLEVLS----GEMLPKPtkgKMRIHCLENVDKALQF 122
Cdd:COG5069    2 EAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQkdnaGEYNETP---ETRIHVMENVSGRLEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  123 LKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIvvqTQEGRETrsAKDALLLWCQMKTAGY-PHVNVTNFTSS 201
Cdd:COG5069   79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI---NEEGELT--KHINLLLWCDEDTGGYkPEVDTFDFFRS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  202 WKDGLAFNALIHKHRPDLIDFDKL--KDSNARHNLEHAFNVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:COG5069  154 WRDGLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKVIGIARLIGVEDIVnVSIPDERSIMTYVSWYIIRFG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  279 KMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKpPKFQE 358
Cdd:COG5069  234 LLEKIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCS-RAPLE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  359 KGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELalrnELIRQEKLEQLARRFDRKAAMRETWL 438
Cdd:COG5069  313 TTDLHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNTHPGQEPL----EEEEKPEIEEFDAEGEFEARVFTFWL 388
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-742 5.22e-35

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 134.11  E-value: 5.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  530 LQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKgyqPCDPQVIQ 609
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG---HPDAEEIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  610 DRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGL 689
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321  690 DAHLEQIFQEAHGMVARKQFGH-PQIEARIKEVSAQWDQLKDLAAFCKKNLQDA 742
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1485-1690 7.68e-34

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 130.64  E-value: 7.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1485 RDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQS 1564
Cdd:cd00176    7 RDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1565 SWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLA 1644
Cdd:cd00176   87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLN 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 67782321 1645 SRAQGLLSAGHPEGEQIIRLQ-GQVDKHYAGLKDVAEERKRKLENMY 1690
Cdd:cd00176  167 ELAEELLEEGHPDADEEIEEKlEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-848 5.53e-32

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 125.25  E-value: 5.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  641 KFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKE 720
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  721 VSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVME 800
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321  801 HLEQQAQGFPEE--FRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEAL 848
Cdd:cd00176  164 SLNELAEELLEEghPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
955-1168 8.28e-32

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated 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: 8.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  955 RVHNYCVDCEETSKWITDKTKVVESTkDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQ 1034
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1035 RQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQ 1114
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321 1115 DSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCL 1168
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
745-954 1.30e-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: 124.10  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  745 FFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFR-DSPDVTHRL 823
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  824 QALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQ 903
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  904 IDGVNLAANSLVESGHP-RSREVKQYQDHLNTRWQAFQTLVSERREAVDSAL 954
Cdd:cd00176  162 LKSLNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
174-279 2.53e-31

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: 119.70  E-value: 2.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    174 SAKDALLLWCQMKTAGY-PHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDS--NARHNLEHAFNVAERQLGI-IP 249
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVpKV 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 67782321    250 LLDPEDVFteNPDEKSIITYVVAFYHYFSK 279
Cdd:pfam00307   82 LIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1798-2005 2.98e-28

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 114.47  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1798 DLHRYFYTGAEILGLIDEKHRELP-EDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEkAEAIQN 1876
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1877 KEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRS 1956
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321 1957 KNFSACLELGESLLQRQHQAS-EEIREKLQQVMSRRKEMNEKWEARWERL 2005
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1170-1379 3.24e-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: 111.38  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1170 FQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKV 1249
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1250 QLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEG 1327
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKeaALASEDLGKDLE-SVEELLKKHKELEEELEAHEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 67782321 1328 WLENIDAEGKQLMDEKPQF-TALVSQKLEALHRLWDELQATTKEKTQHLSAAR 1379
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
177-273 5.26e-27

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: 107.02  E-value: 5.26e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     177 DALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDS----NARHNLEHAFNVAERQLGIIPLLD 252
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     253 PEDVFTENPDEKSIITYVVAF 273
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
55-159 5.36e-25

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 101.59  E-value: 5.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     55 VQKKTFTKWVNSHLAR--VSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFL-KEQRVHLE 131
Cdd:pfam00307    2 ELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 67782321    132 NMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1691-1901 1.29e-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: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1691 HLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIAE 1770
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAH-EERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1771 WKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHREL-PEDVGLDASTAESFHRVHTAFERELHLLG 1849
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALaSEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321 1850 VQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVD 1901
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
637-741 1.61e-23

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: 97.00  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    637 KRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEA 716
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321    717 RIKEVSAQWDQLKDLAAFCKKNLQD 741
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
58-156 9.25e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 94.69  E-value: 9.25e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321      58 KTFTKWVNSHLARVSCR-ITDLYKDLRDGRMLIKLLEVLSGEMLPK--PTKGKMRIHCLENVDKALQFLKEQRVHLENMG 134
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 67782321     135 SHDIVDGNHrLVLGLIWTIILR 156
Cdd:smart00033   81 PEDLVEGPK-LILGVIWTLISL 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
422-525 1.69e-19

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: 85.45  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    422 QLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITA 501
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 67782321    502 RKDNILRLWSYLQELLQSRRQRLE 525
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1690-1793 1.96e-19

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: 85.45  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1690 YHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIA 1769
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAH-QDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....
gi 67782321   1770 EWKDGLNEMWADLLELIDTRMQLL 1793
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
640-740 2.34e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 85.07  E-value: 2.34e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     640 WKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIK 719
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     720 EVSAQWDQLKDLAAFCKKNLQ 740
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1906-2006 3.01e-19

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: 85.06  E-value: 3.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1906 FRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQ 1985
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 67782321   1986 QVMSRRKEMNEKWEARWERLR 2006
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
425-525 1.18e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.07  E-value: 1.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     425 RRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKD 504
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     505 NILRLWSYLQELLQSRRQRLE 525
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1584-1688 2.23e-17

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: 79.67  E-value: 2.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1584 NEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIR 1663
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321   1664 LQGQVDKHYAGLKDVAEERKRKLEN 1688
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1907-2005 3.11e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.91  E-value: 3.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1907 RFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQ 1986
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 67782321    1987 VMSRRKEMNEKWEARWERL 2005
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
743-846 4.32e-17

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: 78.90  E-value: 4.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    743 ENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGF-PEEFRDSPDVTH 821
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321    822 RLQALRELYQQVVAQADLRQQRLQE 846
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
2182-2279 4.56e-16

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 76.31  E-value: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   2182 EGYLGRKHDLEGPNKKAS--NRSWNNLYCVLRNSELTFYKDAKNLAlgmPYHGEEP----------LALRHAICEIAANY 2249
Cdd:pfam15410    3 KGIVMRKCCFESKGKKTPrgKRSWKMVYAVLKDLVLYLYKDEHPPE---SSQFEDKkslknapvgkIRLHHALATPAPDY 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 67782321   2250 KKKKHVFKLRLSNGSEWLFHGKDEEEMLSW 2279
Cdd:pfam15410   80 TKKSHVFRLQTADGAEYLFQTGSPKELQEW 109
SPEC smart00150
Spectrin repeats;
1482-1580 5.88e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.44  E-value: 5.88e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1482 QISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGH 1561
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 67782321    1562 LQSSWDRLREAAAGRLQRL 1580
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1274-1375 1.88e-15

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: 74.28  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1274 LELQNFLQNCQELTLWINDK--LLTSQDVSYD--EARNLHNKwlkHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTAL 1349
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKeaLLSSEDYGKDleSVQALLKK---HKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*.
gi 67782321   1350 VSQKLEALHRLWDELQATTKEKTQHL 1375
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
1694-1793 2.21e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.90  E-value: 2.21e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1694 QLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIAEWKD 1773
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAH-EERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 67782321    1774 GLNEMWADLLELIDTRMQLL 1793
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1062-1166 6.53e-15

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: 72.74  E-value: 6.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1062 QLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQtDPEYLLLGQ 1141
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321   1142 RLEGLDTGWNALGRMWESRSHTLAQ 1166
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2179-2288 1.18e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 71.81  E-value: 1.18e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    2179 VQMEGYLGRKhdlegpnKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHgeePLALRHAICEIAANYK--KKKHVF 2256
Cdd:smart00233    1 VIKEGWLYKK-------SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKG---SIDLSGCTVREAPDPDssKKPHCF 70
                            90       100       110
                    ....*....|....*....|....*....|..
gi 67782321    2257 KLRLSNGSEWLFHGKDEEEMLSWLQGVSTAIN 2288
Cdd:smart00233   71 EIKTSDRKTLLLQAESEEEREKWVEALRKAIA 102
SPEC smart00150
Spectrin repeats;
1064-1164 2.44e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.82  E-value: 2.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1064 QAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQtDPEYLLLGQRL 1143
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 67782321    1144 EGLDTGWNALGRMWESRSHTL 1164
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
747-845 4.55e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 4.55e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     747 QFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEF-RDSPDVTHRLQA 825
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhPDAEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 67782321     826 LRELYQQVVAQADLRQQRLQ 845
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
851-951 4.92e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 4.92e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     851 YTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQD 930
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     931 HLNTRWQAFQTLVSERREAVD 951
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1277-1375 7.26e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.28  E-value: 7.26e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1277 QNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKL 1354
Cdd:smart00150    1 QQFLRDADELEAWLEEKeqLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 67782321    1355 EALHRLWDELQATTKEKTQHL 1375
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
848-949 1.06e-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: 66.19  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    848 LDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQ 927
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|..
gi 67782321    928 YQDHLNTRWQAFQTLVSERREA 949
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQK 102
SPEC smart00150
Spectrin repeats;
1385-1475 2.58e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 2.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1385 LQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEK------ 1458
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEErleeln 83
                            90
                    ....*....|....*...
gi 67782321    1459 -RFLDLLEPLGRRKKQLE 1475
Cdd:smart00150   84 eRWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2013-2070 3.94e-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: 53.09  E-value: 3.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321   2013 QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEK 2070
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
302-412 4.26e-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: 53.09  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    302 KMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAfstYRTVEKPPKFQEkGNLEVLlfTIQSRMRANNQKVY 381
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELAAHQ-DRVEAL--NELAEKLIDEGHYA 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 67782321    382 TPHDGKLVSDINRAWESLEEAEYRRELALRN 412
Cdd:pfam00435   75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2013-2070 1.22e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 1.22e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321    2013 QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEK 2070
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNE 59
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1389-1475 6.44e-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: 49.62  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1389 ADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKR-------FL 1461
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERleelnerWE 90
                           90
                   ....*....|....
gi 67782321   1462 DLLEPLGRRKKQLE 1475
Cdd:pfam00435   91 QLLELAAERKQKLE 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1321-2010 8.36e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 8.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1321 ELASHEGWLENIDAEGKQLMDEKPQftalVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHadlNKWISAMED 1400
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ---LEELEAQLE 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1401 QLRSDdPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIE---KRFLDLLEPLGRRKKQLESS 1477
Cdd:TIGR02168  327 ELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERL 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1478 RAKLQisrDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEE 1557
Cdd:TIGR02168  406 EARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1558 RLGHLQSSWDRLreaaagrlQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDE--EGAIVMLKRHLRQQRAVED 1635
Cdd:TIGR02168  483 ELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyEAAIEAALGGRLQAVVVEN 554
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1636 ---YGRNIKQLASRAQG--------LLSAGHPEGEQIIRLQGQvdKHYAGLKDVAEERKRKLEN-MYHLFQLKRETDDLE 1703
Cdd:TIGR02168  555 lnaAKKAIAFLKQNELGrvtflpldSIKGTEIQGNDREILKNI--EGFLGVAKDLVKFDPKLRKaLSYLLGGVLVVDDLD 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1704 QWIsekelvASSPEMGQDFDHVTLLRDKFR--------DFARETGAIGQER-VDNVNAFIERL---IDAGHSEAATIAEW 1771
Cdd:TIGR02168  633 NAL------ELAKKLRPGYRIVTLDGDLVRpggvitggSAKTNSSILERRReIEELEEKIEELeekIAELEKALAELRKE 706
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1772 KDGLNEMWADLL-ELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEdvgLDASTAESFHRVHTAFERELHLLGV 1850
Cdd:TIGR02168  707 LEELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAE 783
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1851 QVQQFQDVATRLQTAYAGEKAEAIQNKE-QEVSAAWQALLDACAGRRTQLVDTADKFRFFS-MARDLLSWMESIIRQIET 1928
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEE 863
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1929 QERPRDVssvellmkyhqgINAEIETRSKNFSACLELGESLLQRQHQASEEIRE------KLQQVMSRRKEMNEKWEARW 2002
Cdd:TIGR02168  864 LEELIEE------------LESELEALLNERASLEEALALLRSELEELSEELREleskrsELRRELEELREKLAQLELRL 931

                   ....*...
gi 67782321   2003 ERLRMLLE 2010
Cdd:TIGR02168  932 EGLEVRID 939
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
677-1042 1.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   677 RKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEA---RIKEVSAQWDQLKDLAAFCKKNLQDAENffqfqgDAD 753
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAveaRREELEDRDEELRDRLEECRVAAQAHNE------EAE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   754 DLKawlQDAHRLLSGEDVGQDEGATraLGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQv 833
Cdd:PRK02224  346 SLR---EDADDLEERAEELREEAAE--LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE- 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   834 vAQADLRQQRLQEALDLYTVfgeTDACElwmgEKEKWLAEMEMPDTLEDLEVVQH---------RFDILDQEMKTLMTQI 904
Cdd:PRK02224  420 -ERDELREREAELEATLRTA---RERVE----EAEALLEAGKCPECGQPVEGSPHvetieedreRVEELEAELEDLEEEV 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   905 DGVNLAANSLVEsghprSREVKQYQDHLNTRWQAFQTLVSERREAVDS-ALRvhnycvdCEETSKWITDKTKVVESTKDL 983
Cdd:PRK02224  492 EEVEERLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEkRER-------AEELRERAAELEAEAEEKREA 559
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67782321   984 GRDLAGII-AIQRKLSGLERDVAAIQARVDALER--ESQQLMDSHPEQKEDIGQRQKHLEEL 1042
Cdd:PRK02224  560 AAEAEEEAeEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAEL 621
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
994-1204 1.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  994 QRKLSGLERDVAAIQARVDALERESQQLmdshpEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDF 1073
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1074 QAWLSI--TQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDtGWN 1151
Cdd:COG4913  684 SDDLAAleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDA 762
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67782321 1152 ALGRMWESRSHTLAQCLGfqEFQKDAKQAEAILS--NQEYTLAHLEPPDSLEAAE 1204
Cdd:COG4913  763 VERELRENLEERIDALRA--RLNRAEEELERAMRafNREWPAETADLDADLESLP 815
 
Name Accession Description Interval E-value
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
25-156 7.72e-84

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: 270.77  E-value: 7.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   25 APDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPT 104
Cdd:cd21317    1 LADDDWDNDNSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  105 KGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21317   81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
40-156 3.66e-83

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: 268.08  E-value: 3.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   40 FERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKA 119
Cdd:cd21246    1 FERSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 67782321  120 LQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21246   81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
170-281 1.54e-82

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: 266.10  E-value: 1.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  170 RETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIP 249
Cdd:cd21319    1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 67782321  250 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 281
Cdd:cd21319   81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
2-156 3.26e-78

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: 255.35  E-value: 3.26e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    2 TSATEFENVGNQPPYSRINARWDApdDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKD 81
Cdd:cd21316    2 TVATDFDNIDIQQQYSDVNNRWDV--DEWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67782321   82 LRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21316   80 LRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
20-156 5.86e-77

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: 251.10  E-value: 5.86e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   20 NARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEM 99
Cdd:cd21318    3 NNRWESTERPWDEPAATAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQ 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 67782321  100 LPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21318   83 LPKPTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
173-277 4.36e-74

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: 241.53  E-value: 4.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21248    1 RSAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                         90       100
                 ....*....|....*....|....*
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21248   81 PEDVNVEQPDEKSIITYVVTYYHYF 105
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
158-287 1.05e-67

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: 224.55  E-value: 1.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  158 QIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHA 237
Cdd:cd21322    1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321  238 FNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEG 287
Cdd:cd21322   81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKALAVEG 130
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
173-277 6.49e-66

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: 218.05  E-value: 6.49e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21194    1 KSAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80
                         90       100
                 ....*....|....*....|....*
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21194   81 AEDVDVARPDEKSIMTYVASYYHYF 105
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
170-288 8.09e-65

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: 215.69  E-value: 8.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  170 RETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIP 249
Cdd:cd21321    1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 67782321  250 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGK 288
Cdd:cd21321   81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGK 119
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
40-156 2.41e-63

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: 211.39  E-value: 2.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   40 FERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKA 119
Cdd:cd21193    1 FEKGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 67782321  120 LQFLKEQrVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21193   81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIILR 116
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
2181-2286 2.50e-55

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 187.82  E-value: 2.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2181 MEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLRL 2260
Cdd:cd10571    1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321 2261 SNGSEWLFHGKDEEEMLSWLQGVSTA 2286
Cdd:cd10571   81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
173-280 9.95e-55

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: 186.46  E-value: 9.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21320    1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
                         90       100
                 ....*....|....*....|....*...
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYFSKM 280
Cdd:cd21320   81 PEDISVDHPDEKSIITYVVTYYHYFSKM 108
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
48-438 3.82e-54

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 201.71  E-value: 3.82e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   48 LADEREVVQKKTFTKWVNSHLARVSC-RITDLYKDLRDGRMLIKLLEVLS----GEMLPKPtkgKMRIHCLENVDKALQF 122
Cdd:COG5069    2 EAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQkdnaGEYNETP---ETRIHVMENVSGRLEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  123 LKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIvvqTQEGRETrsAKDALLLWCQMKTAGY-PHVNVTNFTSS 201
Cdd:COG5069   79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI---NEEGELT--KHINLLLWCDEDTGGYkPEVDTFDFFRS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  202 WKDGLAFNALIHKHRPDLIDFDKL--KDSNARHNLEHAFNVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:COG5069  154 WRDGLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKVIGIARLIGVEDIVnVSIPDERSIMTYVSWYIIRFG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  279 KMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKpPKFQE 358
Cdd:COG5069  234 LLEKIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCS-RAPLE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  359 KGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELalrnELIRQEKLEQLARRFDRKAAMRETWL 438
Cdd:COG5069  313 TTDLHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNTHPGQEPL----EEEEKPEIEEFDAEGEFEARVFTFWL 388
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
173-279 7.25e-53

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: 181.21  E-value: 7.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21249    3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                         90       100
                 ....*....|....*....|....*..
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYFSK 279
Cdd:cd21249   83 PEDVAVPHPDERSIMTYVSLYYHYFSK 109
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
174-277 9.36e-53

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: 180.67  E-value: 9.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21189    1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21189   81 EDVDVPEPDEKSIITYVSSLYDVF 104
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
159-278 3.72e-52

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: 179.10  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  159 IQDIVVqtqegrETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAF 238
Cdd:cd21216    1 IQDISV------EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAF 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 67782321  239 NVAERQLGIIPLLDPED-VFTENPDEKSIITYVVAFYHYFS 278
Cdd:cd21216   75 DVAEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAFA 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
55-158 2.78e-47

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: 164.88  E-value: 2.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRVHLENMG 134
Cdd:cd21188    3 VQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR-ERGRMRFHRLQNVQTALDFLKYRKIKLVNIR 81
                         90       100
                 ....*....|....*....|....
gi 67782321  135 SHDIVDGNHRLVLGLIWTIILRFQ 158
Cdd:cd21188   82 AEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
55-160 2.13e-43

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: 154.08  E-value: 2.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCR-ITDLYKDLRDGRMLIKLLEVLSGEMLpKPTKGKMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21186    2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKL-KPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                         90       100
                 ....*....|....*....|....*..
gi 67782321  134 GSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21186   81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
178-277 2.14e-42

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: 150.96  E-value: 2.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  178 ALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPED-V 256
Cdd:cd21253    5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmV 84
                         90       100
                 ....*....|....*....|.
gi 67782321  257 FTENPDEKSIITYVVAFYHYF 277
Cdd:cd21253   85 ALKVPDKLSILTYVSQYYNYF 105
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
179-274 6.85e-42

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: 149.50  E-value: 6.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  179 LLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFT 258
Cdd:cd21187    5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
                         90
                 ....*....|....*.
gi 67782321  259 ENPDEKSIITYVVAFY 274
Cdd:cd21187   85 EQPDKKSILMYVTSLF 100
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
171-278 4.67e-41

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: 147.67  E-value: 4.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  171 ETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPL 250
Cdd:cd21291    7 EGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQL 86
                         90       100
                 ....*....|....*....|....*....
gi 67782321  251 LDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:cd21291   87 LDVEDVCdVAKPDERSIMTYVAYYFHAFS 115
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
49-167 1.50e-40

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: 146.67  E-value: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   49 ADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21236   11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQV 89
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 67782321  129 HLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQ 167
Cdd:cd21236   90 KLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
174-277 2.23e-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: 145.54  E-value: 2.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21243    5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21243   85 EDVDVDKPDEKSIMTYVAQFLKKY 108
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
40-159 2.51e-40

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: 146.06  E-value: 2.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   40 FERSRIKALADEREVVQKKTFTKWVNSHLARVSCRI--TDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVD 117
Cdd:cd21247    5 YEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFLENNS 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 67782321  118 KALQFLKeQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21247   85 KAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
51-160 2.56e-40

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: 145.21  E-value: 2.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNSHLARVS--CRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKM--RIHCLENVDKALQFLKEQ 126
Cdd:cd21241    1 EQERVQKKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKLPC-EKGRRlkRVHFLSNINTALKFLESK 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 67782321  127 RVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21241   80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
55-157 1.07e-39

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: 143.31  E-value: 1.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPK-PTKGKMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21215    4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRyNKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
                         90       100
                 ....*....|....*....|....
gi 67782321  134 GSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21215   84 GAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
53-155 1.09e-39

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: 143.30  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   53 EVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21214    3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKLVS 82
                         90       100
                 ....*....|....*....|...
gi 67782321  133 MGSHDIVDGNHRLVLGLIWTIIL 155
Cdd:cd21214   83 IGAEEIVDGNLKMTLGMIWTIIL 105
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
156-278 7.67e-39

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: 141.76  E-value: 7.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  156 RFQIQDIVVqtqegrETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLE 235
Cdd:cd21290    1 RFAIQDISV------EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLN 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 67782321  236 HAFNVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:cd21290   75 NAFEVAEKYLDIPKMLDAEDIVnTARPDEKAIMTYVSSFYHAFS 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
174-277 9.27e-39

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 140.51  E-value: 9.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21239    1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDP 79
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21239   80 EDVDVSSPDEKSVITYVSSLYDVF 103
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
50-167 1.29e-38

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: 140.93  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   50 DEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRVH 129
Cdd:cd21235    1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQ 167
Cdd:cd21235   80 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 117
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
177-278 1.62e-38

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: 139.73  E-value: 1.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  177 DALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDV 256
Cdd:cd22198    3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
                         90       100
                 ....*....|....*....|...
gi 67782321  257 FT-ENPDEKSIITYVVAFYHYFS 278
Cdd:cd22198   83 ASlAVPDKLSMVSYLSQFYEAFK 105
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
173-277 5.53e-38

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: 138.33  E-value: 5.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21192    2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                         90       100
                 ....*....|....*....|....*
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21192   82 VEDVLVDKPDERSIMTYVSQFLRMF 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
174-278 8.87e-38

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: 137.86  E-value: 8.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21200    1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                         90       100
                 ....*....|....*....|....*..
gi 67782321  254 ED--VFTENPDEKSIITYVVAFYHYFS 278
Cdd:cd21200   81 EDmvRMGNRPDWKCVFTYVQSLYRHLR 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
50-160 1.62e-36

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: 134.28  E-value: 1.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   50 DEREVVQKKTFTKWVNSHLARVSCR-ITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21231    1 YEREDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVK-EKGSTRVHALNNVNKALQVLQKNNV 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 67782321  129 HLENMGSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21231   80 DLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
50-167 7.88e-36

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: 132.85  E-value: 7.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   50 DEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRVH 129
Cdd:cd21237    1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVK 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQ 167
Cdd:cd21237   80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
159-278 9.54e-36

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: 132.90  E-value: 9.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  159 IQDIVVqtqegrETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAF 238
Cdd:cd21287    1 IQDISV------EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAF 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 67782321  239 NVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:cd21287   75 DVAEKYLDIPKMLDAEDIVgTARPDEKAIMTYVSSFYHAFS 115
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
178-277 2.05e-35

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: 131.12  E-value: 2.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  178 ALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVF 257
Cdd:cd21197    4 ALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMV 83
                         90       100
                 ....*....|....*....|.
gi 67782321  258 TEN-PDEKSIITYVVAFYHYF 277
Cdd:cd21197   84 TMHvPDRLSIITYVSQYYNHF 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
174-277 3.75e-35

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: 130.55  E-value: 3.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERqLGIIPLLDP 253
Cdd:cd21240    4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 82
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21240   83 EDVDVPSPDEKSVITYVSSIYDAF 106
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
174-277 4.56e-35

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: 130.34  E-value: 4.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21244    5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21244   85 EDVDVVNPDEKSIMTYVAQFLQYS 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-742 5.22e-35

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 134.11  E-value: 5.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  530 LQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKgyqPCDPQVIQ 609
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG---HPDAEEIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  610 DRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGL 689
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321  690 DAHLEQIFQEAHGMVARKQFGH-PQIEARIKEVSAQWDQLKDLAAFCKKNLQDA 742
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
51-160 8.40e-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: 129.61  E-value: 8.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNSHLARVS--CRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKM-RIHCLENVDKALQFLKEQR 127
Cdd:cd21190    1 EQERVQKKTFTNWINSHLAKLSqpIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLqRAHKLSNIRNALDFLTKRC 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 67782321  128 VHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21190   81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
174-274 9.92e-35

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: 129.37  E-value: 9.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21238    2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 81
                         90       100
                 ....*....|....*....|.
gi 67782321  254 EDVFTENPDEKSIITYVVAFY 274
Cdd:cd21238   82 EDVDVPQPDEKSIITYVSSLY 102
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
159-278 1.13e-34

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: 129.84  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  159 IQDIVVqtqegrETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAF 238
Cdd:cd21289    1 IQDISV------EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAF 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 67782321  239 NVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:cd21289   75 EVAEKYLDIPKMLDAEDIVnTPKPDEKAIMTYVSCFYHAFA 115
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
179-274 3.67e-34

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 127.74  E-value: 3.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  179 LLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDK-LKDSNARHNLEHAFNVAERQLGIIPLLDPEDVF 257
Cdd:cd21233    5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
                         90
                 ....*....|....*..
gi 67782321  258 TENPDEKSIITYVVAFY 274
Cdd:cd21233   85 TAHPDKKSILMYVTSLF 101
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
174-277 4.23e-34

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: 127.48  E-value: 4.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQlGIIPLLDP 253
Cdd:cd21199    8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLTI 86
                         90       100
                 ....*....|....*....|....*
gi 67782321  254 ED-VFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21199   87 DEmVSMERPDWQSVMSYVTAIYKHF 111
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
175-279 5.38e-34

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: 127.29  E-value: 5.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  175 AKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPE 254
Cdd:cd21252    1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321  255 D-VFTENPDEKSIITYVVAFYHYFSK 279
Cdd:cd21252   81 DmVSMKVPDCLSIMTYVSQYYNHFSN 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1485-1690 7.68e-34

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 130.64  E-value: 7.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1485 RDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQS 1564
Cdd:cd00176    7 RDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1565 SWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLA 1644
Cdd:cd00176   87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLN 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 67782321 1645 SRAQGLLSAGHPEGEQIIRLQ-GQVDKHYAGLKDVAEERKRKLENMY 1690
Cdd:cd00176  167 ELAEELLEEGHPDADEEIEEKlEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
423-636 9.13e-34

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 130.26  E-value: 9.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  423 LARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITAR 502
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  503 KDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGD 582
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321  583 KVKAITAATLKFTEGKgyQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQS 636
Cdd:cd00176  161 RLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
159-278 1.08e-32

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: 124.03  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  159 IQDIVVqtqegrETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAF 238
Cdd:cd21288    1 IQDISV------EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAM 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 67782321  239 NVAERQLGIIPLLDPEDVF-TENPDEKSIITYVVAFYHYFS 278
Cdd:cd21288   75 EIAEKHLDIPKMLDAEDIVnTPKPDERAIMTYVSCFYHAFA 115
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-848 5.53e-32

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 125.25  E-value: 5.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  641 KFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKE 720
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  721 VSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVME 800
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321  801 HLEQQAQGFPEE--FRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEAL 848
Cdd:cd00176  164 SLNELAEELLEEghPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
955-1168 8.28e-32

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated 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: 8.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  955 RVHNYCVDCEETSKWITDKTKVVESTkDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQ 1034
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1035 RQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQ 1114
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321 1115 DSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCL 1168
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
745-954 1.30e-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: 124.10  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  745 FFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFR-DSPDVTHRL 823
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  824 QALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQ 903
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321  904 IDGVNLAANSLVESGHP-RSREVKQYQDHLNTRWQAFQTLVSERREAVDSAL 954
Cdd:cd00176  162 LKSLNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
179-274 1.31e-31

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: 120.06  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  179 LLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFT 258
Cdd:cd21234    5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
                         90
                 ....*....|....*.
gi 67782321  259 ENPDEKSIITYVVAFY 274
Cdd:cd21234   85 QLPDKKSIIMYLTSLF 100
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
174-278 2.26e-31

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: 119.45  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21198    1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
                         90       100
                 ....*....|....*....|....*.
gi 67782321  254 ED-VFTENPDEKSIITYVVAFYHYFS 278
Cdd:cd21198   80 ADmVLLSVPDKLSVMTYLHQIRAHFT 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
174-279 2.53e-31

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: 119.70  E-value: 2.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    174 SAKDALLLWCQMKTAGY-PHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDS--NARHNLEHAFNVAERQLGI-IP 249
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVpKV 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 67782321    250 LLDPEDVFteNPDEKSIITYVVAFYHYFSK 279
Cdd:pfam00307   82 LIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
173-277 2.59e-31

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: 119.76  E-value: 2.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKdaLLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21195    5 RPSK--LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTT 82
                         90       100
                 ....*....|....*....|....*.
gi 67782321  253 PEDVFT-ENPDEKSIITYVVAFYHYF 277
Cdd:cd21195   83 GKEMASaQEPDKLSMVMYLSKFYELF 108
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
51-160 3.34e-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: 119.17  E-value: 3.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNSHLARVSCR--ITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21242    1 EQEQTQKRTFTNWINSQLAKHSPPsvVSDLFTDIQDGHRLLDLLEVLSGQQLPR-EKGHNVFQCRSNIETALSFLKNKSI 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 67782321  129 HLENMGSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21242   80 KLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
55-160 4.19e-31

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


Pssm-ID: 409081  Cd Length: 107  Bit Score: 118.96  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARV-SCRITDLYKDLRDGRMLIKLLEVLSGEMLPKpTKGKMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21232    2 VQKKTFTKWINARFSKSgKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                         90       100
                 ....*....|....*....|....*..
gi 67782321  134 GSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21232   81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
55-159 9.37e-30

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: 115.08  E-value: 9.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKG-KMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21227    4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKpLNQHQKLENVTLALKAMAEDGIKLVNI 83
                         90       100
                 ....*....|....*....|....*.
gi 67782321  134 GSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21227   84 GNEDIVNGNLKLILGLIWHLILRYQI 109
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
179-279 1.25e-29

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: 114.59  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  179 LLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD-PEDVF 257
Cdd:cd21250    9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                         90       100
                 ....*....|....*....|..
gi 67782321  258 TENPDEKSIITYVVAFYHYFSK 279
Cdd:cd21250   89 AEEPDKLSMVMYLSKFYELFRG 110
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
173-277 1.38e-29

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: 114.66  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKdaLLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21251    6 RSSK--LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMT 83
                         90       100
                 ....*....|....*....|....*.
gi 67782321  253 PEDVFT-ENPDEKSIITYVVAFYHYF 277
Cdd:cd21251   84 GKEMASvGEPDKLSMVMYLTQFYEMF 109
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
177-277 9.03e-29

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: 112.17  E-value: 9.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  177 DALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDV 256
Cdd:cd21226    3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                         90       100
                 ....*....|....*....|.
gi 67782321  257 FTENPDEKSIITYVVAFYHYF 277
Cdd:cd21226   83 MTGNPDERSIVLYTSLFYHAF 103
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
173-278 9.13e-29

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: 112.19  E-value: 9.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  173 RSAKDALLLWCQMKTAGYpHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21245    2 RKAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHYFS 278
Cdd:cd21245   81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
174-279 1.99e-28

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: 111.29  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21258    1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                         90       100
                 ....*....|....*....|....*...
gi 67782321  254 ED--VFTENPDEKSIITYVVAFYHYFSK 279
Cdd:cd21258   81 EDmmIMGKKPDSKCVFTYVQSLYNHLRR 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1798-2005 2.98e-28

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 114.47  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1798 DLHRYFYTGAEILGLIDEKHRELP-EDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEkAEAIQN 1876
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1877 KEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRS 1956
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321 1957 KNFSACLELGESLLQRQHQAS-EEIREKLQQVMSRRKEMNEKWEARWERL 2005
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1904-2070 3.87e-28

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 114.08  E-value: 3.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1904 DKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREK 1983
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1984 LQQVMSRRKEMNEKWEARWERLRMLLEVCQFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAE 2063
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                 ....*..
gi 67782321 2064 RFAALEK 2070
Cdd:cd00176  161 RLKSLNE 167
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1585-1797 6.50e-28

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 113.69  E-value: 6.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1585 EAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRL 1664
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1665 QGQVDKHYAGLKDVAEERKRKLENMYHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQ 1744
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-E 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321 1745 ERVDNVNAFIERLIDAGHSEA-ATIAEWKDGLNEMWADLLELIDTRMQLLAASY 1797
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
51-161 7.61e-28

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: 109.98  E-value: 7.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNSHLARVS--CRITDLYKDLRDGRMLIKLLEVLSG-EMLPKPTKGKMRIHCLENVDKALQFLKEQR 127
Cdd:cd21191    1 ERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGqNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 67782321  128 VHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQD 161
Cdd:cd21191   81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
174-277 2.40e-27

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: 108.19  E-value: 2.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21257    8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                         90       100
                 ....*....|....*....|....*
gi 67782321  254 ED-VFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21257   87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
176-274 2.59e-27

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: 108.25  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  176 KDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPED 255
Cdd:cd21260    3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                         90       100
                 ....*....|....*....|
gi 67782321  256 -VFTENPDEKSIITYVVAFY 274
Cdd:cd21260   83 mVRMSVPDSKCVYTYIQELY 102
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1170-1379 3.24e-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: 111.38  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1170 FQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKV 1249
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1250 QLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEG 1327
Cdd:cd00176   82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKeaALASEDLGKDLE-SVEELLKKHKELEEELEAHEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 67782321 1328 WLENIDAEGKQLMDEKPQF-TALVSQKLEALHRLWDELQATTKEKTQHLSAAR 1379
Cdd:cd00176  161 RLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
174-274 3.51e-27

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: 107.77  E-value: 3.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21259    1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                         90       100
                 ....*....|....*....|..
gi 67782321  254 ED-VFTENPDEKSIITYVVAFY 274
Cdd:cd21259   81 EDmVRMREPDWKCVYTYIQEFY 102
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
849-1069 4.23e-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: 111.38  E-value: 4.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  849 DLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQY 928
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  929 QDHLNTRWQAFQTLVSERREAVDSALRVHNYCVDCEETSKWITDKTKVVESTkDLGRDLAGIIAIQRKLSGLERDVAAIQ 1008
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67782321 1009 ARVDALERESQQLMDS-HPEQKEDIGQRQKHLEELWqglqqslqgqEDLLGEVSQLQAFLQD 1069
Cdd:cd00176  160 PRLKSLNELAEELLEEgHPDADEEIEEKLEELNERW----------EELLELAEERQKKLEE 211
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
177-273 5.26e-27

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: 107.02  E-value: 5.26e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     177 DALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDS----NARHNLEHAFNVAERQLGIIPLLD 252
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     253 PEDVFTENPDEKSIITYVVAF 273
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
46-159 5.70e-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: 107.54  E-value: 5.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   46 KALADERE--VVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKG-KMRIHCLENVDKALQF 122
Cdd:cd21311    4 RDLAEDAQwkRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRpTFRSQKLENVSVALKF 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  123 LK-EQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21311   84 LEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
55-157 8.64e-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: 106.41  E-value: 8.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRI--HCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21183    4 IQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFqqHYLENVSTALKFIEADHIKLVN 83
                         90       100
                 ....*....|....*....|....*
gi 67782321  133 MGSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21183   84 IGSGDIVNGNIKLILGLIWTLILHY 108
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
174-270 1.27e-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: 106.03  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21255    1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
                         90
                 ....*....|....*...
gi 67782321  254 ED-VFTENPDEKSIITYV 270
Cdd:cd21255   80 ADmVLLPIPDKLIVMTYL 97
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
174-277 1.39e-25

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: 103.61  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21256   14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
                         90       100
                 ....*....|....*....|....*
gi 67782321  254 ED-VFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21256   93 NEmVRTERPDWQSVMTYVTAIYKYF 117
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
174-278 2.04e-25

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: 102.62  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAErQLGIIPLLDP 253
Cdd:cd21254    1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
                         90       100
                 ....*....|....*....|....*.
gi 67782321  254 ED-VFTENPDEKSIITYVVAFYHYFS 278
Cdd:cd21254   80 SDmVLLAVPDKLTVMTYLYQIRAHFS 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1385-1584 4.14e-25

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.61  E-value: 4.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1385 LQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEK------ 1458
Cdd:cd00176    6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQErleeln 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1459 -RFLDLLEPLGRRKKQLESSRAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDV 1537
Cdd:cd00176   86 qRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 67782321 1538 LQRGQQLVEAAEID-CQDLEERLGHLQSSWDRLREAAAGRLQRLRDAN 1584
Cdd:cd00176  166 NELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
174-277 4.69e-25

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: 101.58  E-value: 4.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21261    1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                         90       100
                 ....*....|....*....|....*.
gi 67782321  254 ED--VFTENPDEKSIITYVVAFYHYF 277
Cdd:cd21261   81 EDmmVMGRKPDPMCVFTYVQSLYNHL 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
55-159 5.36e-25

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 101.59  E-value: 5.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     55 VQKKTFTKWVNSHLAR--VSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFL-KEQRVHLE 131
Cdd:pfam00307    2 ELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 67782321    132 NMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
55-157 6.29e-25

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: 6.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGK--MRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21228    4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRptFRQMKLENVSVALEFLERESIKLVS 83
                         90       100
                 ....*....|....*....|....*
gi 67782321  133 MGSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21228   84 IDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
174-276 1.68e-24

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: 99.62  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTagyPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21184    1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
                         90       100
                 ....*....|....*....|....
gi 67782321  253 PEDVFTENPDEKSIITYVVAFYHY 276
Cdd:cd21184   78 PEDMVSPNVDELSVMTYLSYFRNA 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1691-1901 1.29e-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: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1691 HLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIAE 1770
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAH-EERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1771 WKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHREL-PEDVGLDASTAESFHRVHTAFERELHLLG 1849
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALaSEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67782321 1850 VQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVD 1901
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
55-159 1.59e-23

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: 97.79  E-value: 1.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEML-----PKPTKGKMRihcLENVDKALQFLKEQRVH 129
Cdd:cd21310   16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkyhPRPNFRQMK---LENVSVALEFLDREHIK 92
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21310   93 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
637-741 1.61e-23

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: 97.00  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    637 KRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEA 716
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321    717 RIKEVSAQWDQLKDLAAFCKKNLQD 741
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1275-1478 1.83e-23

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.60  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1275 ELQNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQ 1352
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKeeLLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1353 KLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRK 1432
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67782321 1433 EELGELFAQVPSMGEEGGDADL--------SIEKRFLDLLEPLGRRKKQLESSR 1478
Cdd:cd00176  160 PRLKSLNELAEELLEEGHPDADeeieekleELNERWEELLELAEERQKKLEEAL 213
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
56-157 5.85e-23

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: 95.34  E-value: 5.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNSHLARVSCR--ITDLYKDLRDGRMLIKLLEVLSGEMLPKP-TKGKMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21212    1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIhSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                         90       100
                 ....*....|....*....|....*
gi 67782321  133 MGSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21212   81 ITAEDIVDGNLKAILGLFFSLSRYK 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
58-156 9.25e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 94.69  E-value: 9.25e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321      58 KTFTKWVNSHLARVSCR-ITDLYKDLRDGRMLIKLLEVLSGEMLPK--PTKGKMRIHCLENVDKALQFLKEQRVHLENMG 134
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 67782321     135 SHDIVDGNHrLVLGLIWTIILR 156
Cdd:smart00033   81 PEDLVEGPK-LILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1062-1265 1.76e-22

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 97.90  E-value: 1.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1062 QLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQ-GQTDPEYLllG 1140
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEeGHPDAEEI--Q 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1141 QRLEGLDTGWNALGRMWESRSHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENN 1220
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 67782321 1221 RDKVLSPVDSGNKLVAEGNLYS-DKIKEKVQLIEDRHRKNNEKAQE 1265
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEE 204
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
53-153 5.82e-20

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: 87.20  E-value: 5.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   53 EVVQKKTFTKWVNSHLARVSC-RITDLYKDLRDGRMLIKLLEVLSGEMLPKPTK--GKMRIHCLENVDKALQFL-KEQRV 128
Cdd:cd21225    2 EKVQIKAFTAWVNSVLEKRGIpKISDLATDLSDGVRLIFFLELVSGKKFPKKFDlePKNRIQMIQNLHLAMLFIeEDLKI 81
                         90       100
                 ....*....|....*....|....*
gi 67782321  129 HLENMGSHDIVDGNHRLVLGLIWTI 153
Cdd:cd21225   82 RVQGIGAEDFVDNNKKLILGLLWTL 106
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
174-277 1.16e-19

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: 86.25  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDP 253
Cdd:cd21196    3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                         90       100
                 ....*....|....*....|....
gi 67782321  254 EDVFTeNPDEKSIITYVVAFYHYF 277
Cdd:cd21196   83 QAVVA-GSDPLGLIAYLSHFHSAF 105
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
55-159 1.49e-19

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: 86.68  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEML-----PKPTKGKMRihcLENVDKALQFLKEQRVH 129
Cdd:cd21308   20 IQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkhnQRPTFRQMQ---LENVSVALEFLDRESIK 96
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21308   97 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
422-525 1.69e-19

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: 85.45  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    422 QLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITA 501
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 67782321    502 RKDNILRLWSYLQELLQSRRQRLE 525
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1690-1793 1.96e-19

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: 85.45  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1690 YHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIA 1769
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAH-QDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....
gi 67782321   1770 EWKDGLNEMWADLLELIDTRMQLL 1793
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
55-159 2.02e-19

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: 86.29  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEML-----PKPTKGKMRihcLENVDKALQFLKEQRVH 129
Cdd:cd21309   17 IQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMyrkyhQRPTFRQMQ---LENVSVALEFLDRESIK 93
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21309   94 LVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
SPEC smart00150
Spectrin repeats;
640-740 2.34e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 85.07  E-value: 2.34e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     640 WKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIK 719
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     720 EVSAQWDQLKDLAAFCKKNLQ 740
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1906-2006 3.01e-19

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: 85.06  E-value: 3.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1906 FRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQ 1985
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 67782321   1986 QVMSRRKEMNEKWEARWERLR 2006
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
176-275 3.30e-19

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: 84.70  E-value: 3.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  176 KDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSN---ARHNLEHAFNVAERQ-LGIIPLL 251
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSpfkKRENINLFLNACKKLgLPELDLF 80
                         90       100
                 ....*....|....*....|....
gi 67782321  252 DPEDVFtENPDEKSIITYVVAFYH 275
Cdd:cd00014   81 EPEDLY-EKGNLKKVLGTLWALAL 103
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
57-155 6.39e-19

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: 83.93  E-value: 6.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   57 KKTFTKWVNSHLA-RVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPK-PTKGKMRIHCLENVDKALQFLKEQRVH-LENM 133
Cdd:cd00014    1 EEELLKWINEVLGeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKiNKKPKSPFKKRENINLFLNACKKLGLPeLDLF 80
                         90       100
                 ....*....|....*....|...
gi 67782321  134 GSHDIV-DGNHRLVLGLIWTIIL 155
Cdd:cd00014   81 EPEDLYeKGNLKKVLGTLWALAL 103
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
2182-2290 7.52e-19

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269955  Cd Length: 113  Bit Score: 83.96  E-value: 7.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2182 EGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPY--HGEEPLALRHAICEIAANYKKKKHVFKLR 2259
Cdd:cd01253    3 EGWLHYKQIVTDKGKRVSDRSWKQAWAVLRGHSLYLYKDKREQTPALSIelGSEQRISIRGCIVDIAYSYTKRKHVFRLT 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 67782321 2260 LSNGSEWLFHGKDEEEMLSWLQgvstAINES 2290
Cdd:cd01253   83 TSDFSEYLFQAEDRDDMLGWIK----AIQEN 109
SPEC smart00150
Spectrin repeats;
425-525 1.18e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.07  E-value: 1.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     425 RRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKD 504
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     505 NILRLWSYLQELLQSRRQRLE 525
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1584-1688 2.23e-17

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: 79.67  E-value: 2.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1584 NEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIR 1663
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321   1664 LQGQVDKHYAGLKDVAEERKRKLEN 1688
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1907-2005 3.11e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.91  E-value: 3.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1907 RFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQ 1986
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 67782321    1987 VMSRRKEMNEKWEARWERL 2005
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
528-635 3.59e-17

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: 78.90  E-value: 3.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    528 LALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYqpcDPQV 607
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHY---ASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 67782321    608 IQDRISHLEQCFEELSNMAAGRKAQLEQ 635
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
743-846 4.32e-17

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: 78.90  E-value: 4.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    743 ENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGF-PEEFRDSPDVTH 821
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321    822 RLQALRELYQQVVAQADLRQQRLQE 846
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
2174-2288 5.95e-17

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270107  Cd Length: 126  Bit Score: 79.30  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2174 DHGQSVQMEGYLGRKHDLEGPNKKAS--NRSWNNLYCVLRNSELTFYKDAKNLALGMPYHG-EEPLALRHAICEIAANYK 2250
Cdd:cd13295    1 DPNAVEYKKGYLMRKCCADPDGKKTPfgKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESlRNAISVHHSLATKATDYT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321 2251 KKKHVFKLRLSNGSEWLFHGKDEEEMLSWLQgvstAIN 2288
Cdd:cd13295   81 KKPHVFRLRTADWREYLFQASDTKEMQSWIE----AIN 114
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
176-279 7.32e-17

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: 78.20  E-value: 7.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  176 KDALLLWCQmktAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPE 254
Cdd:cd21229    5 KKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                         90       100
                 ....*....|....*....|....*
gi 67782321  255 DVFTENPDEKSIITYVvafyHYFSK 279
Cdd:cd21229   82 DLSSPHLDELSGMTYL----SYFMK 102
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
174-273 1.07e-16

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: 77.42  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWCQMKTagyPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAERQLGIIPLLD 252
Cdd:cd21230    1 TPKQRLLGWIQNKI---PQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                         90       100
                 ....*....|....*....|.
gi 67782321  253 PEDVFTENPDEKSIITYVVAF 273
Cdd:cd21230   78 PEEIINPNVDEMSVMTYLSQF 98
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
2182-2279 4.56e-16

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 76.31  E-value: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   2182 EGYLGRKHDLEGPNKKAS--NRSWNNLYCVLRNSELTFYKDAKNLAlgmPYHGEEP----------LALRHAICEIAANY 2249
Cdd:pfam15410    3 KGIVMRKCCFESKGKKTPrgKRSWKMVYAVLKDLVLYLYKDEHPPE---SSQFEDKkslknapvgkIRLHHALATPAPDY 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 67782321   2250 KKKKHVFKLRLSNGSEWLFHGKDEEEMLSW 2279
Cdd:pfam15410   80 TKKSHVFRLQTADGAEYLFQTGSPKELQEW 109
SPEC smart00150
Spectrin repeats;
1482-1580 5.88e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.44  E-value: 5.88e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1482 QISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGH 1561
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 67782321    1562 LQSSWDRLREAAAGRLQRL 1580
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
56-149 7.28e-16

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 75.41  E-value: 7.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNSHLA-RVSCR-ITDLYKDLRDGRMLIKLLEVLSGEMLP----KP-TKGKMRihclENVDKALQFLKEQRV 128
Cdd:cd21213    1 QLQAYVAWVNSQLKkRPGIRpVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPtTDAERK----ENVEKVLQFMASKRI 76
                         90       100
                 ....*....|....*....|....*
gi 67782321  129 HLENMGSHDIVDGN----HRLVLGL 149
Cdd:cd21213   77 RMHQTSAKDIVDGNlkaiMRLILAL 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1274-1375 1.88e-15

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: 74.28  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1274 LELQNFLQNCQELTLWINDK--LLTSQDVSYD--EARNLHNKwlkHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTAL 1349
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKeaLLSSEDYGKDleSVQALLKK---HKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*.
gi 67782321   1350 VSQKLEALHRLWDELQATTKEKTQHL 1375
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
1587-1687 1.98e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.90  E-value: 1.98e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1587 QQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQG 1666
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321    1667 QVDKHYAGLKDVAEERKRKLE 1687
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1694-1793 2.21e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.90  E-value: 2.21e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1694 QLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIgQERVDNVNAFIERLIDAGHSEAATIAEWKD 1773
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAH-EERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 67782321    1774 GLNEMWADLLELIDTRMQLL 1793
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1062-1166 6.53e-15

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: 72.74  E-value: 6.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1062 QLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQtDPEYLLLGQ 1141
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 67782321   1142 RLEGLDTGWNALGRMWESRSHTLAQ 1166
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2179-2288 1.18e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 71.81  E-value: 1.18e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    2179 VQMEGYLGRKhdlegpnKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHgeePLALRHAICEIAANYK--KKKHVF 2256
Cdd:smart00233    1 VIKEGWLYKK-------SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKG---SIDLSGCTVREAPDPDssKKPHCF 70
                            90       100       110
                    ....*....|....*....|....*....|..
gi 67782321    2257 KLRLSNGSEWLFHGKDEEEMLSWLQGVSTAIN 2288
Cdd:smart00233   71 EIKTSDRKTLLLQAESEEEREKWVEALRKAIA 102
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
49-159 1.49e-14

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: 71.93  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   49 ADEREvvqKKTFTKWVNSHLarVSCRITDLYKDLRDGRMLIKLLE-----VLSGEMLPKPTKgKMRIHCLENVDKALQFL 123
Cdd:cd21219    1 EGSRE---ERAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKP-LNKFKKVENCNYAVDLA 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTIIlRFQI 159
Cdd:cd21219   75 KKLGFSLVGIGGKDIADGNRKLTLALVWQLM-RYHV 109
SPEC smart00150
Spectrin repeats;
1064-1164 2.44e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.82  E-value: 2.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1064 QAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQtDPEYLLLGQRL 1143
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 67782321    1144 EGLDTGWNALGRMWESRSHTL 1164
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
747-845 4.55e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 4.55e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     747 QFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEF-RDSPDVTHRLQA 825
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhPDAEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 67782321     826 LRELYQQVVAQADLRQQRLQ 845
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1482-1582 4.70e-14

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: 70.04  E-value: 4.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1482 QISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGH 1561
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|.
gi 67782321   1562 LQSSWDRLREAAAGRLQRLRD 1582
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
851-951 4.92e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 70.05  E-value: 4.92e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     851 YTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQD 930
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 67782321     931 HLNTRWQAFQTLVSERREAVD 951
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1277-1375 7.26e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.28  E-value: 7.26e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1277 QNFLQNCQELTLWINDK--LLTSQDVSYDEArNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKL 1354
Cdd:smart00150    1 QQFLRDADELEAWLEEKeqLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 67782321    1355 EALHRLWDELQATTKEKTQHL 1375
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
177-270 2.92e-13

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: 68.87  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  177 DALLLWCQMKTAGYpHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKD----------------------------- 227
Cdd:cd21224    3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQpttqtvdraqdeaedfwvaefspstgdsg 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 67782321  228 ------SNARHNLeHAFNVAERQLGIIPLLDPEDVFTEN-PDEKSIITYV 270
Cdd:cd21224   82 lssellANEKRNF-KLVQQAVAELGGVPALLRASDMSNTiPDEKVVILFL 130
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
51-160 7.95e-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: 66.88  E-value: 7.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNShLArVSCRITDLYKDLRDGRMLIKLLEVLSGEML--------PKPTKGKMRihCLENVDKALQF 122
Cdd:cd21298    2 IEETREEKTYRNWMNS-LG-VNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkpFKKLGANMK--KIENCNYAVEL 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  123 LKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQ 160
Cdd:cd21298   78 GKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
848-949 1.06e-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: 66.19  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    848 LDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQ 927
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|..
gi 67782321    928 YQDHLNTRWQAFQTLVSERREA 949
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQK 102
SPEC smart00150
Spectrin repeats;
957-1043 1.19e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.81  E-value: 1.19e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     957 HNYCVDCEETSKWITDKTKVVESTkDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQ 1036
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                    ....*..
gi 67782321    1037 KHLEELW 1043
Cdd:smart00150   80 EELNERW 86
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
2182-2289 1.32e-12

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 66.15  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2182 EGYLGRKHDLEGPNKKasNRSWNNLYCVLRNSELTFYKDAKNLAL-GMPY-HGEEPLALRHAICEIAANYKKKKHVFKLR 2259
Cdd:cd13233    3 QGLLNKTKIAENGKKL--RKNWSTSWVVLTSSHLLFYKDAKSAAKsGNPYsKPESSVDLRGASIEWAKEKSSRKNVFQIS 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321 2260 LSNGSEWLFHGKDEEEMLSWLQGVSTAINE 2289
Cdd:cd13233   81 TVTGTEFLLQSDNDTEIREWFDAIKAVIQR 110
SPEC smart00150
Spectrin repeats;
531-634 2.79e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.04  E-value: 2.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321     531 QKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGkgyQPCDPQVIQD 610
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 67782321     611 RISHLEQCFEELSNMAAGRKAQLE 634
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
51-159 3.76e-12

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 65.14  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVvqkKTFTKWVNShlARVSCRITDLYKDLRDGRMLIKLLE-VLSGEML------PKPTKGKMRIHCLENVDKALQFL 123
Cdd:cd21300    6 EREA---RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSVNwkkvnkAPASAEISRFKAVENTNYAVELG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTiILRFQI 159
Cdd:cd21300   81 KQLGFSLVGIQGADITDGSRTLTLALVWQ-LMRFHI 115
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
165-273 7.26e-12

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: 64.32  E-value: 7.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  165 QTQEGRETRSAKDALLLWCQMKTagyPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAER 243
Cdd:cd21314    2 EDEEDARKQTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADD 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321  244 QLGIIPLLDPEDVFTENPDEKSIITYVVAF 273
Cdd:cd21314   79 WLGVPQVIAPEEIVDPNVDEHSVMTYLSQF 108
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1797-1901 1.06e-11

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: 63.49  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1797 YDLHRYFYTGAEILGLIDEKHREL-PEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLqTAYAGEKAEAIQ 1875
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLsSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 67782321   1876 NKEQEVSAAWQALLDACAGRRTQLVD 1901
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1171-1265 1.07e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 1.07e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1171 QEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQ 1250
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|....*
gi 67782321    1251 LIEDRHRKNNEKAQE 1265
Cdd:smart00150   81 ELNERWEELKELAEE 95
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
167-273 3.05e-11

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: 62.49  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  167 QEGRETRSAKDALLLWCQMKTagyPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAERQL 245
Cdd:cd21315    9 PDDGKGPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWL 85
                         90       100
                 ....*....|....*....|....*...
gi 67782321  246 GIIPLLDPEDVFTENPDEKSIITYVVAF 273
Cdd:cd21315   86 DVPQLIKPEEMVNPKVDELSMMTYLSQF 113
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
954-1043 3.68e-11

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: 61.95  E-value: 3.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    954 LRVHNYCVDCEETSKWITDKTKVVEStKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIG 1033
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
                           90
                   ....*....|
gi 67782321   1034 QRQKHLEELW 1043
Cdd:pfam00435   80 ERLEELNERW 89
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
57-154 3.91e-11

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 62.21  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   57 KKTFTKWVNSHLAR---VSCRIT------DLYKDLRDGRMLIKLLEVLSGEMLP--KPTKGKMR--IHCLENVDKALQFL 123
Cdd:cd21217    3 KEAFVEHINSLLADdpdLKHLLPidpdgdDLFEALRDGVLLCKLINKIVPGTIDerKLNKKKPKniFEATENLNLALNAA 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTII 154
Cdd:cd21217   83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
74-154 8.75e-11

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: 61.07  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   74 RITDLYKDLRDGRMLIKLLEVLSGemlPKPTKGKMRIHC------LENVDKALQFLKEQRVHLENMGSH----DIVDGNH 143
Cdd:cd21223   25 AVTNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVPAisrlqkLHNVEVALKALKEAGVLRGGDGGGitakDIVDGHR 101
                         90
                 ....*....|.
gi 67782321  144 RLVLGLIWTII 154
Cdd:cd21223  102 EKTLALLWRII 112
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
58-153 1.36e-10

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: 60.43  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   58 KTFTKWVNSHLARVSCR--ITDLYKDLRDGRMLIKLLEVLSGEML------PKpTKGKMrihcLENVDKALQFLKEQRVH 129
Cdd:cd21286    3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVedingcPR-SQSQM----IENVDVCLSFLAARGVN 77
                         90       100
                 ....*....|....*....|....
gi 67782321  130 LENMGSHDIVDGNHRLVLGLIWTI 153
Cdd:cd21286   78 VQGLSAEEIRNGNLKAILGLFFSL 101
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
168-273 1.18e-09

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: 57.79  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  168 EGRETRSAKDALLLWCQMKTagyPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAERQLG 246
Cdd:cd21313    2 DDAKKQTPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLG 78
                         90       100
                 ....*....|....*....|....*..
gi 67782321  247 IIPLLDPEDVFTENPDEKSIITYVVAF 273
Cdd:cd21313   79 VPQVITPEEIIHPDVDEHSVMTYLSQF 105
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
165-273 1.28e-09

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: 57.89  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  165 QTQEGRETRSAKDALLLWCQMKtagYPHVNVTNFTSSWKDGLAFNALIHKHRPDLI-DFDKLKDSNARHNLEHAFNVAER 243
Cdd:cd21312    3 EEDEEAKKQTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADD 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 67782321  244 QLGIIPLLDPEDVFTENPDEKSIITYVVAF 273
Cdd:cd21312   80 WLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
191-275 1.47e-09

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: 56.93  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  191 PHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNvAERQLGIIPLLDPEDVFTENPDEKSIITYV 270
Cdd:cd21185   15 PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYA 93

                 ....*
gi 67782321  271 VAFYH 275
Cdd:cd21185   94 AQLQK 98
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
56-159 5.79e-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: 55.97  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNShlARVSCRITDLYKDLRDGRMLIKLLE-----VLSGEMLPKPTKgKMRIHCLENVDKALQFLKEQRVHL 130
Cdd:cd21299    5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPI-KMPFKKVENCNQVVKIGKQLKFSL 81
                         90       100
                 ....*....|....*....|....*....
gi 67782321  131 ENMGSHDIVDGNHRLVLGLIWTiILRFQI 159
Cdd:cd21299   82 VNVAGNDIVQGNKKLILALLWQ-LMRYHM 109
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2179-2287 9.87e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 9.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   2179 VQMEGYLGRKHDLEGpnkkasnRSWNNLYCVLRNSELTFYKDaknlalGMPYHGEEP---LALRHAICEI--AANYKKKK 2253
Cdd:pfam00169    1 VVKEGWLLKKGGGKK-------KSWKKRYFVLFDGSLLYYKD------DKSGKSKEPkgsISLSGCEVVEvvASDSPKRK 67
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 67782321   2254 HVFKLRLS---NGSEWLFHGKDEEEMLSWLQGVSTAI 2287
Cdd:pfam00169   68 FCFELRTGertGKRTYLLQAESEEERKDWIKAIQSAI 104
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
56-153 1.53e-08

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


Pssm-ID: 409134  Cd Length: 121  Bit Score: 54.97  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNSHLARVSCR--ITDLYKDLRDGRMLIKLLEVLSGEMLpKPTKG--KMRIHCLENVDKALQFLKEQRVHLE 131
Cdd:cd21285   11 DKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKI-EDINGcpKNRSQMIENIDACLSFLAAKGINIQ 89
                         90       100
                 ....*....|....*....|..
gi 67782321  132 NMGSHDIVDGNHRLVLGLIWTI 153
Cdd:cd21285   90 GLSAEEIRNGNLKAILGLFFSL 111
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
189-257 2.11e-08

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 53.46  E-value: 2.11e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321    189 GYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDK--------LKDSnaRHNLEHAFNVAERQLGI-IPLLDPEDVF 257
Cdd:pfam11971    7 LPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDiclkesmsLADS--LYNIQLLQEFCQRHLGNrCCHLTLEDLL 82
SPEC smart00150
Spectrin repeats;
1385-1475 2.58e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.49  E-value: 2.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1385 LQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEK------ 1458
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEErleeln 83
                            90
                    ....*....|....*...
gi 67782321    1459 -RFLDLLEPLGRRKKQLE 1475
Cdd:smart00150   84 eRWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2013-2070 3.94e-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: 53.09  E-value: 3.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321   2013 QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEK 2070
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
302-412 4.26e-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: 53.09  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    302 KMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAfstYRTVEKPPKFQEkGNLEVLlfTIQSRMRANNQKVY 381
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELAAHQ-DRVEAL--NELAEKLIDEGHYA 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 67782321    382 TPHDGKLVSDINRAWESLEEAEYRRELALRN 412
Cdd:pfam00435   75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
174-263 4.30e-08

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: 53.46  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  174 SAKDALLLWC--QMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDK----LKDSNARHNLEHAFNVAERqLGI 247
Cdd:cd21218   10 PPEEILLRWVnyHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELvlevLSEEDLEKRAEKVLQAAEK-LGC 88
                         90
                 ....*....|....*.
gi 67782321  248 IPLLDPEDVFTENPDE 263
Cdd:cd21218   89 KYFLTPEDIVSGNPRL 104
SPEC smart00150
Spectrin repeats;
1800-1899 6.45e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 6.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    1800 HRYFYTGAEILGLIDEKHREL-PEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAyAGEKAEAIQNKE 1878
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLaSEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 67782321    1879 QEVSAAWQALLDACAGRRTQL 1899
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
2013-2070 1.22e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 1.22e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 67782321    2013 QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEK 2070
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNE 59
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
51-159 1.28e-07

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: 52.70  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNShlARVSCRITDLYKDLRDGRMLIKLLEVLSGEM----LPKPTKGKM--RIHCLENVDKALQFLK 124
Cdd:cd21331   18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKVPVdwnkVNKPPYPKLgaNMKKLENCNYAVELGK 95
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321  125 EQ-RVHLENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21331   96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
56-156 2.01e-07

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 51.68  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNSHLAR---VSCRI---TD---LYKDLRDGRMLIKLL-----EVLSGEML---PKPTKGKMRIHCLENVDK 118
Cdd:cd21294    7 ERREFTKHINAVLAGdpdVGSRLpfpTDtfqLFDECKDGLVLSKLIndsvpDTIDERVLnkpPRKNKPLNNFQMIENNNI 86
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  119 ALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILR 156
Cdd:cd21294   87 VINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRR 124
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
62-153 2.57e-07

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: 51.15  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   62 KWVNSHLARV---SCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKM--RIHCLENVDKALQFLKE--QRVHLEnmg 134
Cdd:cd21218   17 RWVNYHLKKAgptKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlsEEDLEKRAEKVLQAAEKlgCKYFLT--- 93
                         90
                 ....*....|....*....
gi 67782321  135 SHDIVDGNHRLVLGLIWTI 153
Cdd:cd21218   94 PEDIVSGNPRLNLAFVATL 112
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
2181-2281 3.76e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 50.23  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2181 MEGYLGRKhdlegpnKKASNRSWNNLYCVLRNSELTFYKDAKNLALGmpYHGEEPLALRHAICEiaANYKKKKHVFKLRL 2260
Cdd:cd00821    1 KEGYLLKR-------GGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYK--PKGSIPLSGILEVEE--VSPKERPHCFELVT 69
                         90       100
                 ....*....|....*....|.
gi 67782321 2261 SNGSEWLFHGKDEEEMLSWLQ 2281
Cdd:cd00821   70 PDGRTYYLQADSEEERQEWLK 90
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1389-1475 6.44e-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: 49.62  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1389 ADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKR-------FL 1461
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERleelnerWE 90
                           90
                   ....*....|....
gi 67782321   1462 DLLEPLGRRKKQLE 1475
Cdd:pfam00435   91 QLLELAAERKQKLE 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1321-2010 8.36e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 8.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1321 ELASHEGWLENIDAEGKQLMDEKPQftalVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHadlNKWISAMED 1400
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ---LEELEAQLE 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1401 QLRSDdPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIE---KRFLDLLEPLGRRKKQLESS 1477
Cdd:TIGR02168  327 ELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERL 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1478 RAKLQisrDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEE 1557
Cdd:TIGR02168  406 EARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1558 RLGHLQSSWDRLreaaagrlQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDE--EGAIVMLKRHLRQQRAVED 1635
Cdd:TIGR02168  483 ELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyEAAIEAALGGRLQAVVVEN 554
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1636 ---YGRNIKQLASRAQG--------LLSAGHPEGEQIIRLQGQvdKHYAGLKDVAEERKRKLEN-MYHLFQLKRETDDLE 1703
Cdd:TIGR02168  555 lnaAKKAIAFLKQNELGrvtflpldSIKGTEIQGNDREILKNI--EGFLGVAKDLVKFDPKLRKaLSYLLGGVLVVDDLD 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1704 QWIsekelvASSPEMGQDFDHVTLLRDKFR--------DFARETGAIGQER-VDNVNAFIERL---IDAGHSEAATIAEW 1771
Cdd:TIGR02168  633 NAL------ELAKKLRPGYRIVTLDGDLVRpggvitggSAKTNSSILERRReIEELEEKIEELeekIAELEKALAELRKE 706
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1772 KDGLNEMWADLL-ELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEdvgLDASTAESFHRVHTAFERELHLLGV 1850
Cdd:TIGR02168  707 LEELEEELEQLRkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAE 783
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1851 QVQQFQDVATRLQTAYAGEKAEAIQNKE-QEVSAAWQALLDACAGRRTQLVDTADKFRFFS-MARDLLSWMESIIRQIET 1928
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEE 863
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1929 QERPRDVssvellmkyhqgINAEIETRSKNFSACLELGESLLQRQHQASEEIRE------KLQQVMSRRKEMNEKWEARW 2002
Cdd:TIGR02168  864 LEELIEE------------LESELEALLNERASLEEALALLRSELEELSEELREleskrsELRRELEELREKLAQLELRL 931

                   ....*...
gi 67782321   2003 ERLRMLLE 2010
Cdd:TIGR02168  932 EGLEVRID 939
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
51-159 1.32e-06

third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409179  Cd Length: 125  Bit Score: 49.60  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNShlARVSCRITDLYKDLRDGRMLIKLLEVLSGEM----LPKPTKGKM--RIHCLENVDKALQFLK 124
Cdd:cd21330    9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVdwnrVNKPPYPKLgeNMKKLENCNYAVELGK 86
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321  125 EQ-RVHLENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21330   87 NKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
57-157 4.98e-06

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 47.58  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   57 KKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLP------KPTKGKMRIHcleNVDKALQFLKEQRVHL 130
Cdd:cd21222   18 KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyhlTPSTDDEKLH---NVKLALELMEDAGIST 94
                         90       100
                 ....*....|....*....|....*..
gi 67782321  131 ENMGSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21222   95 PKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
56-154 7.10e-06

first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409141  Cd Length: 145  Bit Score: 48.04  E-value: 7.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNSHLAR-VSCR--------ITDLYKDLRDGRMLIKLLEVLSGEMLPKPT--KGKM---RIHclENVDKALQ 121
Cdd:cd21292   25 EKVAFVNWINKNLGDdPDCKhllpmdpnTDDLFEKVKDGILLCKMINLSVPDTIDERAinKKKLtvfTIH--ENLTLALN 102
                         90       100       110
                 ....*....|....*....|....*....|...
gi 67782321  122 FLKEQRVHLENMGSHDIVDGNHRLVLGLIWTII 154
Cdd:cd21292  103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
51-159 1.44e-05

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: 46.52  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   51 EREVVQKKTFTKWVNShlARVSCRITDLYKDLRDGRMLIKLLEVLS-----GEMLPKPTK---GKMRIhcLENVDKALQF 122
Cdd:cd21329    2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTRvpvdwGHVNKPPYPalgGNMKK--IENCNYAVEL 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67782321  123 LKEQ-RVHLENMGSHDIVDGNHRLVLGLIWTIILRFQI 159
Cdd:cd21329   78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
2173-2286 1.75e-05

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 45.73  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2173 RDHGQSVQMEGYLgrkHDLEGpnkkASNRSWNNLYCVLRNSELTFYKDAKN-LALGM----PYHGEEPLALRHAiceiaa 2247
Cdd:cd13248    1 RDPNAPVVMSGWL---HKQGG----SGLKNWRKRWFVLKDNCLYYYKDPEEeKALGSillpSYTISPAPPSDEI------ 67
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 67782321 2248 nykKKKHVFKLRLSNGSEWLFHGKDEEEMLSWLQGVSTA 2286
Cdd:cd13248   68 ---SRKFAFKAEHANMRTYYFAADTAEEMEQWMNAMSLA 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
411-1067 3.06e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    411 RNELIRQEKLEQLARRFDRKAAMRETWLSENQRLvaqdnfgydLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEK 490
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDEL---------AEELAELEEKLEELKEELESLEAELEELEAELEELES 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    491 ENYHDQKRITARKDNILRLwsYLQ-ELLQSRRQRLETTL-----ALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVE 564
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQL--ELQiASLNNEIERLEARLerledRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    565 DLLQKHKLMEADIAIQGDKVKAITAATLKFTEgkgyqpcDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFF- 643
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILg 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    644 --WEMDEAES-WIKEKEqiyssLDYGKDLTSVLI--LQRKHKAFEdelrgldaHLEQIFQEAHGMVARKQFGHPQIEARI 718
Cdd:TIGR02168  524 vlSELISVDEgYEAAIE-----AALGGRLQAVVVenLNAAKKAIA--------FLKQNELGRVTFLPLDSIKGTEIQGND 590
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    719 KEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGD----ADDLKAWLQDAHRLLSGEDV----------------GQDEGAT 778
Cdd:TIGR02168  591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitgGSAKTNS 670
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    779 RALGKKHKdfLEELEESRGVME----HLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALdlytvf 854
Cdd:TIGR02168  671 SILERRRE--IEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV------ 742
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    855 gETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNt 934
Cdd:TIGR02168  743 -EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA- 820
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321    935 rwQAFQTLVSERREAVDSALRVhnycvdcEETSKWITDKTKVVESTKDLGRDL-AGIIAIQRKLSGLERDVAAIQARVDA 1013
Cdd:TIGR02168  821 --NLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELeELIEELESELEALLNERASLEEALAL 891
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 67782321   1014 LERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFL 1067
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
56-154 3.71e-05

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 45.82  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNS---------HLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCL---ENVDKALQFL 123
Cdd:cd21325   25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 104
                         90       100       110
                 ....*....|....*....|....*....|.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTII 154
Cdd:cd21325  105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
56-154 5.45e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 45.42  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNS---------HLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCL---ENVDKALQFL 123
Cdd:cd21323   25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKKKLTPFtisENLNLALNSA 104
                         90       100       110
                 ....*....|....*....|....*....|.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTII 154
Cdd:cd21323  105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
56-154 8.11e-05

first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409173  Cd Length: 145  Bit Score: 45.00  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   56 QKKTFTKWVNS---------HLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCL---ENVDKALQFL 123
Cdd:cd21324   25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 104
                         90       100       110
                 ....*....|....*....|....*....|.
gi 67782321  124 KEQRVHLENMGSHDIVDGNHRLVLGLIWTII 154
Cdd:cd21324  105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1170-1255 8.33e-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: 43.85  E-value: 8.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   1170 FQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKV 1249
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82

                   ....*.
gi 67782321   1250 QLIEDR 1255
Cdd:pfam00435   83 EELNER 88
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
677-1042 1.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   677 RKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEA---RIKEVSAQWDQLKDLAAFCKKNLQDAENffqfqgDAD 753
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAveaRREELEDRDEELRDRLEECRVAAQAHNE------EAE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   754 DLKawlQDAHRLLSGEDVGQDEGATraLGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQv 833
Cdd:PRK02224  346 SLR---EDADDLEERAEELREEAAE--LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE- 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   834 vAQADLRQQRLQEALDLYTVfgeTDACElwmgEKEKWLAEMEMPDTLEDLEVVQH---------RFDILDQEMKTLMTQI 904
Cdd:PRK02224  420 -ERDELREREAELEATLRTA---RERVE----EAEALLEAGKCPECGQPVEGSPHvetieedreRVEELEAELEDLEEEV 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   905 DGVNLAANSLVEsghprSREVKQYQDHLNTRWQAFQTLVSERREAVDS-ALRvhnycvdCEETSKWITDKTKVVESTKDL 983
Cdd:PRK02224  492 EEVEERLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEkRER-------AEELRERAAELEAEAEEKREA 559
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67782321   984 GRDLAGII-AIQRKLSGLERDVAAIQARVDALER--ESQQLMDSHPEQKEDIGQRQKHLEEL 1042
Cdd:PRK02224  560 AAEAEEEAeEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAEL 621
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
58-229 5.57e-04

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 45.32  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   58 KTFTKWVNSHLarVSCRITDLYKDLRDGRMLIKLLEVLSGEM---------LPKPTKGKMRIHCLENVDKALQFLKEQRV 128
Cdd:COG5069  382 RVFTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPMtvthklvkkQPASGIEENRFKAFENENYAVDLGITEGF 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  129 HLENMGSHDIVDGNhRLVLGLIWTiILRFQIQdiVVQTQEGRETRSAKDALLLWC--QMKTAGYPHVNVTNF--TSSWKD 204
Cdd:COG5069  460 SLVGIKGLEILDGI-RLKLTLVWQ-VLRSNTA--LFNHVLKKDGCGLSDSDLCAWlgSLGLKGDKEEGIRSFgdPAGSVS 535
                        170       180
                 ....*....|....*....|....*
gi 67782321  205 GLAFNALIHKHRPDLIDFDKLKDSN 229
Cdd:COG5069  536 GVFYLDVLKGIHSELVDYDLVTRGF 560
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
2179-2294 6.54e-04

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 41.07  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2179 VQMEGYLgrkhdlegpNKKASNR-SWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALrhAICEIaanyKKKKHVFK 2257
Cdd:cd13298    6 VLKSGYL---------LKRSRKTkNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSELLAV--APLKD----KKRKNVFG 70
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 67782321 2258 LrLSNGSEWLFHGKDEEEMLSWLQgvstAINESQSIR 2294
Cdd:cd13298   71 I-YTPSKNLHFRATSEKDANEWVE----ALREEFRLD 102
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
2167-2259 9.44e-04

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 41.07  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2167 ATLPAPRDHgqsVQMEGYLgrkhdlegpNKKAS-NRSWNNLYCVLRNSELTFYKDAKNlalgmPYHGEEPLALRHAI-CE 2244
Cdd:cd13215   12 AYLPKRSGA---VIKSGYL---------SKRSKrTLRYTRYWFVLKGDTLSWYNSSTD-----LYFPAGTIDLRYATsIE 74
                         90
                 ....*....|....*
gi 67782321 2245 IAANYKKKKHVFKLR 2259
Cdd:cd13215   75 LSKSNGEATTSFKIV 89
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
57-143 1.10e-03

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 40.72  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   57 KKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTK---GKMRIHCLENVDKALQFLkeqrVHLENM 133
Cdd:cd21221    3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVaqsEEGQKQKLAVVLACVNFL----LGLEED 78
                         90
                 ....*....|
gi 67782321  134 GSHDIVDGNH 143
Cdd:cd21221   79 EARWTVDGIY 88
PH_CNK_insect-like cd13326
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
2182-2280 1.10e-03

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from insects, spiders, mollusks, and nematodes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270135  Cd Length: 91  Bit Score: 40.02  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2182 EGYLGRKhdlegPNKKASNRSWNNLYCVLRNSELTFYKDAKNL-ALGMpyhgeepLALRHAICEIAANYKKKKHVFKLRL 2260
Cdd:cd13326    2 QGWLYQR-----RRKGKGGGKWAKRWFVLKGSNLYGFRSQESTkADCV-------IFLPGFTVSPAPEVKSRKYAFKVYH 69
                         90       100
                 ....*....|....*....|
gi 67782321 2261 SnGSEWLFHGKDEEEMLSWL 2280
Cdd:cd13326   70 T-GTVFYFAAESQEDMKKWL 88
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
46-158 1.13e-03

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 40.80  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   46 KALADEREVVqKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLP------KPTKGKMRIHcleNVDKA 119
Cdd:cd21307    8 KLGPDKVNTV-KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsefflTPSSTSEMLH---NVTLA 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 67782321  120 LQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQ 158
Cdd:cd21307   84 LELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
994-1204 1.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  994 QRKLSGLERDVAAIQARVDALERESQQLmdshpEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDF 1073
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 1074 QAWLSI--TQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDtGWN 1151
Cdd:COG4913  684 SDDLAAleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDA 762
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67782321 1152 ALGRMWESRSHTLAQCLGfqEFQKDAKQAEAILS--NQEYTLAHLEPPDSLEAAE 1204
Cdd:COG4913  763 VERELRENLEERIDALRA--RLNRAEEELERAMRafNREWPAETADLDADLESLP 815
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
55-157 4.28e-03

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


Pssm-ID: 409155  Cd Length: 121  Bit Score: 39.32  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   55 VQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLP------KPTKGKMRIHcleNVDKALQFLKEQRV 128
Cdd:cd21306   16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhsfhlTPTSFEQKVH---NVQFAFELMQDAGL 92
                         90       100
                 ....*....|....*....|....*....
gi 67782321  129 HLENMGSHDIVDGNHRLVLGLIWTIILRF 157
Cdd:cd21306   93 PKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
62-121 4.76e-03

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: 38.76  E-value: 4.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   62 KWVNSHLArvSCRITDLYKDLRDGRMLIKLLEVLSGEMLPkPTKGKMRIHCLENVDKALQ 121
Cdd:cd21184    8 EWVNSKIP--EYKVKNFTTDWNDGKALAALVDALKPGLIP-DNESLDKENPLENATKAMD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
458-1111 5.07e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  458 EAA------KKKHEAIE--TDTAAYEERVralEDLAQELEK------------ENYHDQKRITARKDNILRLWSYlqELL 517
Cdd:COG1196  163 EAAgiskykERKEEAERklEATEENLERL---EDILGELERqleplerqaekaERYRELKEELKELEAELLLLKL--REL 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  518 QSRRQRLETTLALQklfqdmlhsidwmdEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEG 597
Cdd:COG1196  238 EAELEELEAELEEL--------------EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  598 KgyqpcdpQVIQDRISHLEQcfeelsnmaagRKAQLEQSKRLWKFfwemdEAESWIKEKEQiyssldygkdltsvliLQR 677
Cdd:COG1196  304 I-------ARLEERRRELEE-----------RLEELEEELAELEE-----ELEELEEELEE----------------LEE 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  678 KHKAFEDELRGLDAHLEQIFQEAHGMVARKQfghpQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENffQFQGDADDLKA 757
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEELLEALRAAAELAAQLEELEE--AEEALLERLER 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  758 WLQDAHRLLSgedvgQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQA 837
Cdd:COG1196  419 LEEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  838 DLRQQRLQEALDLYT----VFGETDACELW--MGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAA 911
Cdd:COG1196  494 LLLLEAEADYEGFLEgvkaALLLAGLRGLAgaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  912 NSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAVDSALRVHNYCV----DCEETSKWITDKTKVVESTKDLGRDL 987
Cdd:COG1196  574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgrtlVAARLEAALRRAVTLAGRLREVTLEG 653
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  988 AGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFL 1067
Cdd:COG1196  654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 67782321 1068 QDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEID 1111
Cdd:COG1196  734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
2174-2287 6.65e-03

Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270111  Cd Length: 102  Bit Score: 38.38  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321 2174 DHGQSVQMEGYLgrkHDLegpnKKASNRSWNNLYCVLRNSELTFYKDAKnlalgmPYHGEEPLALRHAI--CEIAANYKK 2251
Cdd:cd13299    1 DDPERVIEQGYL---QVL----KKKGVNQWKKYWLVLRNRSLSFYKDQS------EYSPVKIIPIDDIIdvVELDPLSKS 67
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321 2252 KKHVFKLrLSNGSEWLFHGKDEEEMLSWLQGVSTAI 2287
Cdd:cd13299   68 KKWCLQI-ITPEKRIRFCADDEESLIKWLGALKSLL 102
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
49-158 7.30e-03

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409186  Cd Length: 129  Bit Score: 38.82  E-value: 7.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321   49 ADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLP------KPTKGKMRIHcleNVDKALQF 122
Cdd:cd21337   14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPlhsfflTPDSFEQKVL---NVSFAFEL 90
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67782321  123 LKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQ 158
Cdd:cd21337   91 MQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
392-911 9.38e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  392 INRAWESLEEAEYRRELALRNELIRQEKLE----QLARRFDRKAAMRETWLSE-----NQRLVAQDNFGYDLAAVEAAKK 462
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEeelaELEEELEELEEELEELEEEleeaeEELEEAEAELAEAEEALLEAEA 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  463 KHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSId 542
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE- 451
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  543 wmDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDK-VKAITAATLKFTEGKGYqpcdpqviqdrishleqcfee 621
Cdd:COG1196  452 --AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAaRLLLLLEAEADYEGFLE--------------------- 508
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  622 lsnmAAGRKAQLEQSKRLWKffwEMDEAESWIKEkeqiyssldYGKDLTSVLILQRKHKAFEDELRGLDA--HLEQ---- 695
Cdd:COG1196  509 ----GVKAALLLAGLRGLAG---AVAVLIGVEAA---------YEAALEAALAAALQNIVVEDDEVAAAAieYLKAakag 572
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  696 --IFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQ 773
Cdd:COG1196  573 raTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67782321  774 DEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALDLYTV 853
Cdd:COG1196  653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 67782321  854 FGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLmtqidG-VNLAA 911
Cdd:COG1196  733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-----GpVNLLA 786
 
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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