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Conserved domains on  [gi|117938332|ref|NP_787030|]
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spectrin beta chain, non-erythrocytic 1 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
3-156 4.69e-91

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: 292.33  E-value: 4.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    3 TTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDL 82
Cdd:cd21316     1 TTVATDFDNIDIQQQYSDVNNRWDVDEWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117938332   83 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 156
Cdd:cd21316    81 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
173-277 3.51e-78

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: 253.09  E-value: 3.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21248     1 RSAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21248    81 PEDVNVEQPDEKSIITYVVTYYHYF 105
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
2199-2304 1.67e-61

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: 205.54  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRL 2278
Cdd:cd10571     1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332 2279 SDGNEYLFQAKDDEEMNTWIQAISSA 2304
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
48-530 1.31e-60

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 220.97  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   48 LADEREAVQKKTFTKWVNSHLARVSC-RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR-MRIHCLENVDKALQFLKE 125
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  126 QRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVEtednkEKKSAKDALLLWCQMKTAGY-PNVNIHNFTTSWRD 204
Cdd:COG5069    82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEE-----GELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  205 GMAFNALIHKHRPDLIDFDKL--KKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFSKMK 281
Cdd:COG5069   157 GLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  282 ALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKpPKFTEKGN 361
Cdd:COG5069   237 KIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCS-RAPLETTD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  362 LEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKaeHERELALRNELIRqeKLEQLARRFDRKAAMRETWLSEN 441
Cdd:COG5069   316 LHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNT--HPGQEPLEEEEKP--EIEEFDAEGEFEARVFTFWLNSL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  442 QRLVSQDNFGFD----LPAVEAATKKHEAIETDIAAYEERVQAVVAVAR--ELEAENY-HDIKRITARKDNVIRLWEYLL 514
Cdd:COG5069   392 DVSPEITNLFGDlrdqLILLQALSKKLMPMTVTHKLVKKQPASGIEENRfkAFENENYaVDLGITEGFSLVGIKGLEILD 471
                         490
                  ....*....|....*....
gi 117938332  515 ---ELLRARRQRLEMNLGL 530
Cdd:COG5069   472 girLKLTLVWQVLRSNTAL 490
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-743 1.49e-40

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 149.90  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  530 LQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGegykPCDPQVI 609
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG----HPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  610 RDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSG 689
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 117938332  690 RSGHFEQAIKEGEDMIAEEHFGS-EKIRERIIYIREQWANLEQLSAIRKKRLEEA 743
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
958-1169 1.98e-36

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 137.96  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  958 QNYHLECNETKSWIREKTKVIESTqDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRL 1037
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1038 AEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEED 1117
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1118 YQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSH 1169
Cdd:cd00176   162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
642-849 9.88e-36

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 136.04  E-value: 9.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  642 KFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIY 721
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  722 IREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTID 801
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 117938332  802 TLHEQASALPQAH--AESPDVKGRLAGIEERCKEMAELTRLRKQALQDTL 849
Cdd:cd00176   164 SLNELAEELLEEGhpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1381-1592 1.73e-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: 135.27  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1381 KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKS-TDEVDSK 1459
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1460 RLTVQTKFMELLEPLSERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQP 1539
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1540 RIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAH 1592
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1593-1805 6.53e-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: 133.73  E-value: 6.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1593 KAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMR 1672
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1673 QSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQ 1752
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-E 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 117938332 1753 ERVDTVNNMADELINSGHSDA-ATIAEWKDGLNEAWADLLELIDTRTQILAASY 1805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1171-1380 9.80e-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: 9.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1171 YQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKV 1250
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1251 DSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSY-DEARNLHSKWLKHQAFMAELASNKEW 1329
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLgKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1330 LDKIEKEGMQLISEKPET-EAVVKEKLTGLHKMWEVLESTTQTKAQRLFDAN 1380
Cdd:cd00176   162 LKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1806-2027 1.19e-31

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.48  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1806 ELHKFYHDAKEIFGRIQDKHKKLP-EELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDkADDIQK 1884
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1885 RENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARN 1964
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1965 DSFTACIELGKSLLARKHYASEeikekllqltEKRKEMIDKWEDRWEWLRLILEVHQFSRDAS 2027
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAD----------EEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
851-1061 2.46e-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: 123.32  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  851 LYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQ 930
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  931 DKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIEStQDLGNDLAGVMALQRKLTGMERDLVAIEA 1010
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1011 KLSDLQKEAEKL-ESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEA 1061
Cdd:cd00176   161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2017-2075 8.95e-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 characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


:

Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 8.95e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 117938332  2017 LEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSA 2075
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEA 59
 
Name Accession Description Interval E-value
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
3-156 4.69e-91

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: 292.33  E-value: 4.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    3 TTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDL 82
Cdd:cd21316     1 TTVATDFDNIDIQQQYSDVNNRWDVDEWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117938332   83 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 156
Cdd:cd21316    81 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
173-277 3.51e-78

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: 253.09  E-value: 3.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21248     1 RSAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21248    81 PEDVNVEQPDEKSIITYVVTYYHYF 105
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
2199-2304 1.67e-61

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: 205.54  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRL 2278
Cdd:cd10571     1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332 2279 SDGNEYLFQAKDDEEMNTWIQAISSA 2304
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
48-530 1.31e-60

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 220.97  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   48 LADEREAVQKKTFTKWVNSHLARVSC-RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR-MRIHCLENVDKALQFLKE 125
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  126 QRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVEtednkEKKSAKDALLLWCQMKTAGY-PNVNIHNFTTSWRD 204
Cdd:COG5069    82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEE-----GELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  205 GMAFNALIHKHRPDLIDFDKL--KKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFSKMK 281
Cdd:COG5069   157 GLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  282 ALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKpPKFTEKGN 361
Cdd:COG5069   237 KIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCS-RAPLETTD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  362 LEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKaeHERELALRNELIRqeKLEQLARRFDRKAAMRETWLSEN 441
Cdd:COG5069   316 LHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNT--HPGQEPLEEEEKP--EIEEFDAEGEFEARVFTFWLNSL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  442 QRLVSQDNFGFD----LPAVEAATKKHEAIETDIAAYEERVQAVVAVAR--ELEAENY-HDIKRITARKDNVIRLWEYLL 514
Cdd:COG5069   392 DVSPEITNLFGDlrdqLILLQALSKKLMPMTVTHKLVKKQPASGIEENRfkAFENENYaVDLGITEGFSLVGIKGLEILD 471
                         490
                  ....*....|....*....
gi 117938332  515 ---ELLRARRQRLEMNLGL 530
Cdd:COG5069   472 girLKLTLVWQVLRSNTAL 490
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-743 1.49e-40

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 149.90  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  530 LQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGegykPCDPQVI 609
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG----HPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  610 RDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSG 689
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 117938332  690 RSGHFEQAIKEGEDMIAEEHFGS-EKIRERIIYIREQWANLEQLSAIRKKRLEEA 743
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
958-1169 1.98e-36

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 137.96  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  958 QNYHLECNETKSWIREKTKVIESTqDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRL 1037
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1038 AEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEED 1117
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1118 YQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSH 1169
Cdd:cd00176   162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
642-849 9.88e-36

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 136.04  E-value: 9.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  642 KFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIY 721
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  722 IREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTID 801
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 117938332  802 TLHEQASALPQAH--AESPDVKGRLAGIEERCKEMAELTRLRKQALQDTL 849
Cdd:cd00176   164 SLNELAEELLEEGhpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1381-1592 1.73e-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: 135.27  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1381 KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKS-TDEVDSK 1459
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1460 RLTVQTKFMELLEPLSERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQP 1539
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1540 RIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAH 1592
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1593-1805 6.53e-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: 133.73  E-value: 6.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1593 KAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMR 1672
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1673 QSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQ 1752
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-E 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 117938332 1753 ERVDTVNNMADELINSGHSDA-ATIAEWKDGLNEAWADLLELIDTRTQILAASY 1805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1171-1380 9.80e-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: 9.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1171 YQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKV 1250
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1251 DSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSY-DEARNLHSKWLKHQAFMAELASNKEW 1329
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLgKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1330 LDKIEKEGMQLISEKPET-EAVVKEKLTGLHKMWEVLESTTQTKAQRLFDAN 1380
Cdd:cd00176   162 LKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1806-2027 1.19e-31

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.48  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1806 ELHKFYHDAKEIFGRIQDKHKKLP-EELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDkADDIQK 1884
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1885 RENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARN 1964
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1965 DSFTACIELGKSLLARKHYASEeikekllqltEKRKEMIDKWEDRWEWLRLILEVHQFSRDAS 2027
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAD----------EEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
851-1061 2.46e-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: 123.32  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  851 LYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQ 930
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  931 DKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIEStQDLGNDLAGVMALQRKLTGMERDLVAIEA 1010
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1011 KLSDLQKEAEKL-ESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEA 1061
Cdd:cd00176   161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
173-279 9.23e-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  Cd Length: 109  Bit Score: 117.77  E-value: 9.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   173 KSAKDALLLWCQMKTAGY-PNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHY--NLQNAFNLAEQHLGLTK 249
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 117938332   250 -LLDPEDIsvDHPDEKSIITYVVTYYHYFSK 279
Cdd:pfam00307   81 vLIEPEDL--VEGDNKSVLTYLASLFRRFQA 109
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
638-742 1.27e-25

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 characteristic 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: 103.17  E-value: 1.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   638 RRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRE 717
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332   718 RIIYIREQWANLEQLSAIRKKRLEE 742
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
54-159 2.94e-24

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  Cd Length: 109  Bit Score: 99.28  E-value: 2.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    54 AVQKKTFTKWVNSHLAR--VSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFL-KEQRVHL 130
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 117938332   131 ENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
177-271 3.37e-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: 95.85  E-value: 3.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    177 DALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKS----NAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80
                            90
                    ....*....|....*....
gi 117938332    253 PEDISVDHPDEKSIITYVV 271
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
58-156 1.13e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 94.69  E-value: 1.13e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332     58 KTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLPK--PTKGRMRIHCLENVDKALQFLKEQRVHLENMG 134
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 117938332    135 SHDIVDGNHrLTLGLIWTIILR 156
Cdd:smart00033   81 PEDLVEGPK-LILGVIWTLISL 101
SPEC smart00150
Spectrin repeats;
641-741 2.36e-22

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 93.55  E-value: 2.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    641 WKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERII 720
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    721 YIREQWANLEQLSAIRKKRLE 741
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1592-1696 5.40e-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 characteristic 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: 84.29  E-value: 5.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1592 HKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISM 1671
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332  1672 RQSKVDKLYAGLKDLAEERRGKLDE 1696
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
849-952 5.95e-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 characteristic 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: 83.91  E-value: 5.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   849 LALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRA 928
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 117938332   929 QQDKLNTRWSQFRELVDRKKDALL 952
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2199-2306 6.47e-19

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  Cd Length: 102  Bit Score: 83.75  E-value: 6.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   2199 MEGFLNRKheweahnKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSevpVSLKEAICEVALDYK--KKKHVFKL 2276
Cdd:smart00233    3 KEGWLYKK-------SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGS---IDLSGCTVREAPDPDssKKPHCFEI 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 117938332   2277 RLSDGNEYLFQAKDDEEMNTWIQAISSAIS 2306
Cdd:smart00233   73 KTSDRKTLLLQAESEEEREKWVEALRKAIA 102
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
2200-2301 8.97e-19

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


Pssm-ID: 434701  Cd Length: 118  Bit Score: 84.02  E-value: 8.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  2200 EGFLNRKHEWEAHNKKASS--RSWHNVYCVINNQEMGFYKDAKSAASgipYHSEVPVSLKEA----------ICEVALDY 2267
Cdd:pfam15410    3 KGIVMRKCCFESKGKKTPRgkRSWKMVYAVLKDLVLYLYKDEHPPES---SQFEDKKSLKNApvgkirlhhaLATPAPDY 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 117938332  2268 KKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAI 2301
Cdd:pfam15410   80 TKKSHVFRLQTADGAEYLFQTGSPKELQEWVDTL 113
SPEC smart00150
Spectrin repeats;
1595-1695 3.21e-18

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 81.99  E-value: 3.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1595 QQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQS 1674
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332   1675 KVDKLYAGLKDLAEERRGKLD 1695
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1485-1590 4.00e-18

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 characteristic 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: 81.60  E-value: 4.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1485 KEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIItDSSSLNAEAIR 1564
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 117938332  1565 QRLADLKQLWGLLIEETEKRHRRLEE 1590
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
745-847 4.08e-18

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 characteristic 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: 81.60  E-value: 4.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   745 LLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQA-HAESPDVKGR 823
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEgHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 117938332   824 LAGIEERCKEMAELTRLRKQALQD 847
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1914-2014 7.75e-18

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 characteristic 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: 80.83  E-value: 7.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1914 FRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLL 1993
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 117938332  1994 QLTEKRKEMIDKWEDRWEWLR 2014
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
1488-1589 1.11e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.45  E-value: 1.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1488 HQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIItDSSSLNAEAIRQRL 1567
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 117938332   1568 ADLKQLWGLLIEETEKRHRRLE 1589
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
422-525 1.65e-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 characteristic 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: 80.06  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   422 QLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITA 501
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 117938332   502 RKDNVIRLWEYLLELLRARRQRLE 525
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
425-525 2.92e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.91  E-value: 2.92e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    425 RRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKD 504
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    505 NVIRLWEYLLELLRARRQRLE 525
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
852-951 2.32e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 76.60  E-value: 2.32e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    852 YKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQD 931
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 117938332    932 KLNTRWSQFRELVDRKKDAL 951
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
957-1060 3.50e-16

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 characteristic 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: 76.20  E-value: 3.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   957 IQNYHLECNETKSWIREKTKVIEStQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSR 1036
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 117938332  1037 LAEISDVWEEMKTTLKNREASLGE 1060
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1065-1165 3.77e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.83  E-value: 3.77e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1065 QQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGE-MVTQGQTDAQYmfLRQR 1143
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEqLIEEGHPDAEE--IEER 78
                            90       100
                    ....*....|....*....|..
gi 117938332   1144 LQALDTGWNELHKMWENRQNLL 1165
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
1172-1272 7.16e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.06  E-value: 7.16e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1172 QQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVD 1251
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332   1252 SIDDRHRKNREAASELLMRLK 1272
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1915-2013 3.17e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 3.17e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1915 RFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLLQ 1994
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 117938332   1995 LTEKRKEMIDKWEDRWEWL 2013
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
747-846 3.53e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 3.53e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    747 HQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQA-HAESPDVKGRLA 825
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEgHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    826 GIEERCKEMAELTRLRKQALQ 846
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1275-1378 2.98e-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 characteristic 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: 70.81  E-value: 2.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1275 RDLQKFLQDCQELSLWINEKM--LTAQDMSYD--EARNLHSKwlkHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAV 1350
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEalLSSEDYGKDleSVQALLKK---HKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 117938332  1351 VKEKLTGLHKMWEVLESTTQTKAQRLFD 1378
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
791-1718 7.62e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.19  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  791 EEITNYRPT-IDTLHEQASALPQAHAESPDVKGRLAGIEERCKE--------MAELTRLRKQA--LQDTLALYKMFSEAD 859
Cdd:COG1196   147 EEIINAKPEeRRKLIEEAAGVSKYKERKEEAERKLERTEENLERledlleelEKQLEKLERQAekAERYQELKAELRELE 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  860 ACELWIDEKEqwlNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQiarqlmhnghpSEKEIRAQQDKLNTRWSQ 939
Cdd:COG1196   227 LALLLAKLKE---LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKS-----------ELEELREELEELQEELLE 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  940 FR-ELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIEST-QDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQK 1017
Cdd:COG1196   293 LKeEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALkEELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1018 EAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGE-ASKLQQFLRDLDDFQSWLSRTQTAIASEDmpntlTE 1096
Cdd:COG1196   373 ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERlSERLEDLKEELKELEAELEELQTELEELN-----EE 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1097 AEKLLTQHENIKNEIDNYEEDYQKMRDmgemvtqgqtdAQYMfLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLR 1176
Cdd:COG1196   448 LEELEEQLEELRDRLKELERELAELQE-----------ELQR-LEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1177 DTKQAEAFLN--NQEYVLAhtempttlegAEAAIKKQEDFM--TTMDANEEKINAVVETGRRLVSDgnINSDRIQEKVDS 1252
Cdd:COG1196   516 GVYGPVAELIkvKEKYETA----------LEAALGNRLQAVvvENEEVAKKAIEFLKENKAGRATF--LPLDRIKPLRSL 583
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1253 IDDRHRKNREAASELLmrlkdnrdlqKFLQDCQELSLWINEKMLTAQDMsyDEARNLHSKwLKHQAFMAELASnkewlDK 1332
Cdd:COG1196   584 KSDAAPGFLGLASDLI----------DFDPKYEPAVRFVLGDTLVVDDL--EQARRLARK-LRIKYRIVTLDG-----DL 645
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1333 IEKEG-MQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKA-ELFTQSCADLDKWLHGLESQIQSDDygk 1410
Cdd:COG1196   646 VEPSGsITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNElRSLEDLLEELRRQLEELERQLEELK--- 722
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1411 dlTSVNILLKKQQMLENQMEVRKKEIEELQSQaqalsqEGKSTDEVDSKRLTVQTKFMELLEPLSERKHNLLASKEIHQF 1490
Cdd:COG1196   723 --RELAALEEELEQLQSRLEELEEELEELEEE------LEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE 794
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1491 NRDVEDEILWVGERMpLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDdifersqniitdSSSLNAEAIRQRLADL 1570
Cdd:COG1196   795 LEELEEELEEAERRL-DALERELESLEQRRERLEQEIEELEEEIEELEEKLD------------ELEEELEELEKELEEL 861
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1571 KQLwgllIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILE-QAVEDYAETVH 1649
Cdd:COG1196   862 KEE----LEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEvELPELEEELEE 937
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117938332 1650 QLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRlfQLNREVDDLEQWIAERE 1718
Cdd:COG1196   938 EYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRE--DLEEAKEKLLEVIEELD 1004
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2017-2075 8.95e-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 characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 8.95e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 117938332  2017 LEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSA 2075
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEA 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
993-1287 1.09e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   993 ALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKttlknreaSLGEASKLQqFLRDLD 1072
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--------DLGEEEQLR-VKEKIG 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1073 DFQSWLSRTQTAIAS-----EDMPNTLTEAE----KLLTQHENIKNEIdnyeEDYQKMRD-MGEMVTQGQtdAQYMFLRQ 1142
Cdd:TIGR02169  298 ELEAEIASLERSIAEkerelEDAEERLAKLEaeidKLLAEIEELEREI----EEERKRRDkLTEEYAELK--EELEDLRA 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1143 RLQALDTG---WNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAflnnQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMD 1219
Cdd:TIGR02169  372 ELEEVDKEfaeTRDELKDYREKLEKLKREINELKRELDRLQEEL----QRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117938332  1220 ANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQEL 1287
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
SPEC smart00150
Spectrin repeats;
2020-2075 2.00e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 2.00e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 117938332   2020 HQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSA 2075
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEA 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1004-1710 2.36e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1004 DLVAIEAKLSDLQKEAEKLESEHpdqaQAILSRLAEISDVWEEMKTTLKNREASLGEA-SKLQQFLRDLDDFQSwlsrtQ 1082
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRLEVSELEEEIEELqKELYALANEISRLEQ-----Q 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1083 TAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMvtqgqtdaqymfLRQRLQALDtgwNELHKMWENRQ 1162
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE------------LKEELESLE---AELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1163 NLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHT--EMPTTLEGAEAAIKKQEDfmttmdANEEKINAVVETGRRLVSDGN 1240
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQ------EIEELLKKLEEAELKELQAEL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1241 INSDRIQEKVDSIDDRHRKNREAASELLMRLKdnRDLQKFLQDCQELSLWIN--EKMLTAQDMSYDEARNL-HSKWLKHQ 1317
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAE--QALDAAERELAQLQARLDslERLQENLEGFSEGVKALlKNQSGLSG 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1318 AF--MAELAS-NKEWLDKIEK---EGMQLI------SEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELF 1385
Cdd:TIGR02168  521 ILgvLSELISvDEGYEAAIEAalgGRLQAVvvenlnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1386 TQSCADLDK-----------WLHGL------------------ESQIQSDD-----------YGKDLTSVNILLKKQQM- 1424
Cdd:TIGR02168  601 LGVAKDLVKfdpklrkalsyLLGGVlvvddldnalelakklrpGYRIVTLDgdlvrpggvitGGSAKTNSSILERRREIe 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1425 -LENQMEVRKKEIEELQSQAQALSQEgksTDEVDSKRLTVQTKFMELLEPLSERKHNLLASKEIHQ----FNRDVEDEIL 1499
Cdd:TIGR02168  681 eLEEKIEELEEKIAELEKALAELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELT 757
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1500 WVGERMPLATSTDHGHNLQTVQLLIKKnQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEA--IRQRLADLKQ---LW 1574
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAanLRERLESLERriaAT 836
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1575 GLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQL--- 1651
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrre 916
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117938332  1652 SKTSRALVADSHPESERISMR----QSKVDKLYAGLKDLAEERRGKLDE-----RHRLFQLNREVDDL 1710
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKEL 984
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1528-1951 2.75e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1528 QTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAE------AIRQRLADlkqlwgllIEETEKRHRRLEEAhkaqqyyFDA 1601
Cdd:PRK02224  338 QAHNEEAESLREDADDLEERAEELREEAAELESEleeareAVEDRREE--------IEELEEEIEELRER-------FGD 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1602 AEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDyAETVHQLSK--TSRALVADShPESERISMRQSKVDKL 1679
Cdd:PRK02224  403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEALLEAGKcpECGQPVEGS-PHVETIEEDRERVEEL 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1680 YAGLKDLaEERRGKLDERH----RLFQLNREVDDLEQ--------------WIAE-REVVAGSHELGQDYEHVTMLQERF 1740
Cdd:PRK02224  481 EAELEDL-EEEVEEVEERLeraeDLVEAEDRIERLEErredleeliaerreTIEEkRERAEELRERAAELEAEAEEKREA 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1741 REFARDTGNIGQERVDTVNNMADEL------INSGHSDAATIAEWKDG---LNEAWADLLELIDTRTQILAASyelhkfy 1811
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELkeriesLERIRTLLAAIADAEDEierLREKREALAELNDERRERLAEK------- 632
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1812 hdakeifgriQDKHKKLPEELgrDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGdkaddiQKRENEVLE 1891
Cdd:PRK02224  633 ----------RERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA------VENELEELE 694
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1892 AWKSLLDACEGRRVRLVDtgdkfrffsmVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMN 1951
Cdd:PRK02224  695 ELRERREALENRVEALEA----------LYDEAEELESMYGDLRAELRQRNVETLERMLN 744
 
Name Accession Description Interval E-value
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
3-156 4.69e-91

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: 292.33  E-value: 4.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    3 TTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDL 82
Cdd:cd21316     1 TTVATDFDNIDIQQQYSDVNNRWDVDEWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117938332   83 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 156
Cdd:cd21316    81 RDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
28-156 5.82e-86

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: 276.55  E-value: 5.82e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   28 DDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR 107
Cdd:cd21317     4 DDWDNDNSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 117938332  108 MRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 156
Cdd:cd21317    84 MRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
40-156 2.21e-84

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: 271.55  E-value: 2.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   40 FERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKA 119
Cdd:cd21246     1 FERSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 117938332  120 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 156
Cdd:cd21246    81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
22-156 1.94e-79

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: 258.42  E-value: 1.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   22 NNRWDVDD--WDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGER 99
Cdd:cd21318     3 NNRWESTErpWDEPAATAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQ 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 117938332  100 LPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 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 3.51e-78

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: 253.09  E-value: 3.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21248     1 RSAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21248    81 PEDVNVEQPDEKSIITYVVTYYHYF 105
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
170-288 4.71e-76

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: 247.66  E-value: 4.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  170 KEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTK 249
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 117938332  250 LLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGK 288
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGK 119
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
158-287 7.58e-74

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: 241.88  E-value: 7.58e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  158 QIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNA 237
Cdd:cd21322     1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 117938332  238 FNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEG 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 4.79e-72

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: 235.77  E-value: 4.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21194     1 KSAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
170-281 2.11e-70

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: 231.43  E-value: 2.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  170 KEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTK 249
Cdd:cd21319     1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 117938332  250 LLDPEDISVDHPDEKSIITYVVTYYHYFSKMK 281
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
173-280 2.07e-69

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: 228.45  E-value: 2.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21320     1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*...
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHYFSKM 280
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYHYFSKM 108
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
40-156 8.13e-65

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: 215.62  E-value: 8.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   40 FERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKA 119
Cdd:cd21193     1 FEKGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 117938332  120 LQFLKEQrVHLENMGSHDIVDGNHRLTLGLIWTIILR 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 ...
2199-2304 1.67e-61

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: 205.54  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRL 2278
Cdd:cd10571     1 MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYTKKKHVFRLKL 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332 2279 SDGNEYLFQAKDDEEMNTWIQAISSA 2304
Cdd:cd10571    81 SDGAEFLFQAKDEEEMNQWVKKISFA 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
48-530 1.31e-60

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 220.97  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   48 LADEREAVQKKTFTKWVNSHLARVSC-RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR-MRIHCLENVDKALQFLKE 125
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  126 QRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVEtednkEKKSAKDALLLWCQMKTAGY-PNVNIHNFTTSWRD 204
Cdd:COG5069    82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEE-----GELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  205 GMAFNALIHKHRPDLIDFDKL--KKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFSKMK 281
Cdd:COG5069   157 GLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  282 ALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKpPKFTEKGN 361
Cdd:COG5069   237 KIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCS-RAPLETTD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  362 LEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKaeHERELALRNELIRqeKLEQLARRFDRKAAMRETWLSEN 441
Cdd:COG5069   316 LHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNT--HPGQEPLEEEEKP--EIEEFDAEGEFEARVFTFWLNSL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  442 QRLVSQDNFGFD----LPAVEAATKKHEAIETDIAAYEERVQAVVAVAR--ELEAENY-HDIKRITARKDNVIRLWEYLL 514
Cdd:COG5069   392 DVSPEITNLFGDlrdqLILLQALSKKLMPMTVTHKLVKKQPASGIEENRfkAFENENYaVDLGITEGFSLVGIKGLEILD 471
                         490
                  ....*....|....*....
gi 117938332  515 ---ELLRARRQRLEMNLGL 530
Cdd:COG5069   472 girLKLTLVWQVLRSNTAL 490
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
159-278 1.13e-54

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: 186.41  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  159 IQDISVEtednkeKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAF 238
Cdd:cd21216     1 IQDISVE------ELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  239 NLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21216    75 DVAEKHLDIPKMLDAEDIvNTPRPDERSVMTYVSCYYHAFA 115
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
172-279 1.49e-54

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: 185.84  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  172 KKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 251
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
                          90       100
                  ....*....|....*....|....*...
gi 117938332  252 DPEDISVDHPDEKSIITYVVTYYHYFSK 279
Cdd:cd21249    82 DPEDVAVPHPDERSIMTYVSLYYHYFSK 109
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
174-277 8.32e-50

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: 172.19  E-value: 8.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....
gi 117938332  254 EDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVF 104
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
53-158 8.43e-50

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: 172.20  E-value: 8.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21188     1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR-ERGRMRFHRLQNVQTALDFLKYRKIKLVN 79
                          90       100
                  ....*....|....*....|....*.
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRFQ 158
Cdd:cd21188    80 IRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
55-160 3.45e-45

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: 159.08  E-value: 3.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLpKPTKGRMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21186     2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKL-KPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 117938332  134 GSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21186    81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
159-278 3.66e-45

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: 159.23  E-value: 3.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  159 IQDIsvetedNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAF 238
Cdd:cd21291     1 IADI------NEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  239 NLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21291    75 DIASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAFS 115
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
179-274 1.26e-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: 151.43  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISV 258
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
                          90
                  ....*....|....*.
gi 117938332  259 DHPDEKSIITYVVTYY 274
Cdd:cd21187    85 EQPDKKSILMYVTSLF 100
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
49-167 6.06e-42

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: 150.52  E-value: 6.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   49 ADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21236    11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQV 89
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 117938332  129 HLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETE 167
Cdd:cd21236    90 KLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
51-160 1.32e-41

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: 149.06  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNSHLARVS--CRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRM--RIHCLENVDKALQFLKEQ 126
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKLPC-EKGRRlkRVHFLSNINTALKFLESK 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 117938332  127 RVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21241    80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
170-277 2.25e-41

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: 148.24  E-value: 2.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  170 KEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTK 249
Cdd:cd21243     1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                          90       100
                  ....*....|....*....|....*...
gi 117938332  250 LLDPEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21243    81 LLDPEDVDVDKPDEKSIMTYVAQFLKKY 108
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
178-277 3.99e-41

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: 147.49  E-value: 3.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  178 ALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPED-I 256
Cdd:cd21253     5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmV 84
                          90       100
                  ....*....|....*....|.
gi 117938332  257 SVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21253    85 ALKVPDKLSILTYVSQYYNYF 105
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
156-278 1.07e-40

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: 146.77  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  156 RFQIQDISVEtednkeKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQ 235
Cdd:cd21290     1 RFAIQDISVE------ETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLN 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 117938332  236 NAFNLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21290    75 NAFEVAEKYLDIPKMLDAEDIvNTARPDEKAIMTYVSSFYHAFS 118
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
530-743 1.49e-40

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 149.90  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  530 LQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGegykPCDPQVI 609
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG----HPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  610 RDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSG 689
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 117938332  690 RSGHFEQAIKEGEDMIAEEHFGS-EKIRERIIYIREQWANLEQLSAIRKKRLEEA 743
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
53-155 1.95e-40

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 145.22  E-value: 1.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKLVS 82
                          90       100
                  ....*....|....*....|...
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIIL 155
Cdd:cd21214    83 IGAEEIVDGNLKMTLGMIWTIIL 105
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
40-159 3.24e-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: 145.67  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   40 FERSRIKALADEREAVQKKTFTKWVNSHLARVSCRI--TDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVD 117
Cdd:cd21247     5 YEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFLENNS 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 117938332  118 KALQFLKeQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21247    85 KAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
53-157 1.81e-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: 142.54  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPK-PTKGRMRIHCLENVDKALQFLKEQRVHLE 131
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRyNKNPKMRVQKLENVNKALEFIKSRGVKLT 81
                          90       100
                  ....*....|....*....|....*.
gi 117938332  132 NMGSHDIVDGNHRLTLGLIWTIILRF 157
Cdd:cd21215    82 NIGAEDIVDGNLKLILGLLWTLILRF 107
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
50-164 4.67e-39

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: 142.09  E-value: 4.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   50 DEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 129
Cdd:cd21235     1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 117938332  130 LENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISV 164
Cdd:cd21235    80 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 114
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
174-277 4.80e-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: 141.28  E-value: 4.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                          90       100
                  ....*....|....*....|....
gi 117938332  254 EDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21239    80 EDVDVSSPDEKSVITYVSSLYDVF 103
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
50-160 2.82e-38

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: 139.29  E-value: 2.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   50 DEREAVQKKTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVK-EKGSTRVHALNNVNKALQVLQKNNV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 117938332  129 HLENMGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21231    80 DLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
159-278 4.23e-38

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: 139.45  E-value: 4.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  159 IQDISVEtednkeKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAF 238
Cdd:cd21287     1 IQDISVE------ETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  239 NLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21287    75 DVAEKYLDIPKMLDAEDIvGTARPDEKAIMTYVSSFYHAFS 115
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
172-277 1.43e-37

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: 137.17  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  172 KKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 251
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332  252 DPEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21192    81 EVEDVLVDKPDERSIMTYVSQFLRMF 106
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
177-278 2.23e-37

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: 136.65  E-value: 2.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  177 DALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI 256
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
                          90       100
                  ....*....|....*....|...
gi 117938332  257 -SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd22198    83 aSLAVPDKLSMVSYLSQFYEAFK 105
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
178-277 3.80e-37

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: 136.13  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  178 ALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDIS 257
Cdd:cd21197     4 ALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMV 83
                          90       100
                  ....*....|....*....|.
gi 117938332  258 VDH-PDEKSIITYVVTYYHYF 277
Cdd:cd21197    84 TMHvPDRLSIITYVSQYYNHF 104
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
50-167 4.26e-37

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: 136.32  E-value: 4.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   50 DEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 129
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 117938332  130 LENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETE 167
Cdd:cd21237    80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
958-1169 1.98e-36

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 137.96  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  958 QNYHLECNETKSWIREKTKVIESTqDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRL 1037
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1038 AEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEED 1117
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1118 YQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSH 1169
Cdd:cd00176   162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
174-274 3.14e-36

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 133.61  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21238     2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 81
                          90       100
                  ....*....|....*....|.
gi 117938332  254 EDISVDHPDEKSIITYVVTYY 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 3.89e-36

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: 133.70  E-value: 3.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  159 IQDISVEtednkeKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAF 238
Cdd:cd21289     1 IQDISVE------ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  239 NLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21289    75 EVAEKYLDIPKMLDAEDIvNTPKPDEKAIMTYVSCFYHAFA 115
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
642-849 9.88e-36

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 136.04  E-value: 9.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  642 KFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIY 721
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  722 IREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTID 801
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 117938332  802 TLHEQASALPQAH--AESPDVKGRLAGIEERCKEMAELTRLRKQALQDTL 849
Cdd:cd00176   164 SLNELAEELLEEGhpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1381-1592 1.73e-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: 135.27  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1381 KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKS-TDEVDSK 1459
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1460 RLTVQTKFMELLEPLSERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQP 1539
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1540 RIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAH 1592
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
175-279 4.45e-35

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: 129.99  E-value: 4.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  175 AKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPE 254
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332  255 D-ISVDHPDEKSIITYVVTYYHYFSK 279
Cdd:cd21252    81 DmVSMKVPDCLSIMTYVSQYYNHFSN 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1593-1805 6.53e-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: 133.73  E-value: 6.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1593 KAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMR 1672
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1673 QSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQ 1752
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-E 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 117938332 1753 ERVDTVNNMADELINSGHSDA-ATIAEWKDGLNEAWADLLELIDTRTQILAASY 1805
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
51-160 7.14e-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: 130.00  E-value: 7.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNSHLARVS--CRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRM-RIHCLENVDKALQFLKEQR 127
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSqpIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLqRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 117938332  128 VHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
159-278 9.98e-35

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: 129.81  E-value: 9.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  159 IQDISVEtednkeKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAF 238
Cdd:cd21288     1 IQDISVE------ETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAM 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  239 NLAEQHLGLTKLLDPEDI-SVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21288    75 EIAEKHLDIPKMLDAEDIvNTPKPDERAIMTYVSCFYHAFA 115
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
170-277 5.54e-34

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: 127.26  E-value: 5.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  170 KEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTK 249
Cdd:cd21244     1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
                          90       100
                  ....*....|....*....|....*...
gi 117938332  250 LLDPEDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21244    81 LLEPEDVDVVNPDEKSIMTYVAQFLQYS 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
745-955 5.77e-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: 131.03  E-value: 5.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  745 LLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQA-HAESPDVKGR 823
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEgHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  824 LAGIEERCKEMAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQAS 903
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117938332  904 RVAVVNQIARQLMHNGHP-SEKEIRAQQDKLNTRWSQFRELVDRKKDALLSAL 955
Cdd:cd00176   161 RLKSLNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
423-638 7.20e-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: 7.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  423 LARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITAR 502
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  503 KDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAE 582
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 117938332  583 RVRGVNASAQKFATDGEgykPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESR 638
Cdd:cd00176   161 RLKSLNELAEELLEEGH---PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1171-1380 9.80e-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: 9.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1171 YQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKV 1250
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1251 DSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSY-DEARNLHSKWLKHQAFMAELASNKEW 1329
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLgKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1330 LDKIEKEGMQLISEKPET-EAVVKEKLTGLHKMWEVLESTTQTKAQRLFDAN 1380
Cdd:cd00176   162 LKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1488-1698 2.91e-33

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 129.10  E-value: 2.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1488 HQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIItDSSSLNAEAIRQRL 1567
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1568 ADLKQLWGLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAET 1647
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1648 VHQLSKTSRALVADSHPES-ERISMRQSKVDKLYAGLKDLAEERRGKLDERH 1698
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
174-277 2.94e-33

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: 125.15  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21240     4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 82
                          90       100
                  ....*....|....*....|....
gi 117938332  254 EDISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21240    83 EDVDVPSPDEKSVITYVSSIYDAF 106
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
179-274 2.66e-32

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: 122.34  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDK-LKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDIS 257
Cdd:cd21233     5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
                          90
                  ....*....|....*..
gi 117938332  258 VDHPDEKSIITYVVTYY 274
Cdd:cd21233    85 TAHPDKKSILMYVTSLF 101
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
174-278 3.02e-32

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: 122.07  E-value: 3.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 117938332  254 EDISV--DHPDEKSIITYVVTYYHYFS 278
Cdd:cd21200    81 EDMVRmgNRPDWKCVFTYVQSLYRHLR 107
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
54-160 3.78e-32

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: 121.65  E-value: 3.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   54 AVQKKTFTKWVNSHLARV-SCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21232     1 DVQKKTFTKWINARFSKSgKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVN 79
                          90       100
                  ....*....|....*....|....*...
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21232    80 IGGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
51-160 5.19e-32

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: 121.48  E-value: 5.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNSHLARVSCR--ITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRV 128
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPsvVSDLFTDIQDGHRLLDLLEVLSGQQLPR-EKGHNVFQCRSNIETALSFLKNKSI 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 117938332  129 HLENMGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21242    80 KLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
179-274 1.11e-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: 120.45  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISV 258
Cdd:cd21234     5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
                          90
                  ....*....|....*.
gi 117938332  259 DHPDEKSIITYVVTYY 274
Cdd:cd21234    85 QLPDKKSIIMYLTSLF 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1806-2027 1.19e-31

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 124.48  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1806 ELHKFYHDAKEIFGRIQDKHKKLP-EELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDkADDIQK 1884
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSsTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1885 RENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARN 1964
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1965 DSFTACIELGKSLLARKHYASEeikekllqltEKRKEMIDKWEDRWEWLRLILEVHQFSRDAS 2027
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDAD----------EEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
851-1061 2.46e-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: 123.32  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  851 LYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQ 930
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  931 DKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIEStQDLGNDLAGVMALQRKLTGMERDLVAIEA 1010
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1011 KLSDLQKEAEKL-ESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEA 1061
Cdd:cd00176   161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1276-1484 5.75e-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: 122.17  E-value: 5.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1276 DLQKFLQDCQELSLWINEKMLTAQDMSY-DEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEK 1354
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1355 LTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKK 1434
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1435 EIEELQSQAQALSQEG--KSTDEVDSKRLTVQTKFMELLEPLSERKHNLLAS 1484
Cdd:cd00176   161 RLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
173-278 5.81e-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: 118.30  E-value: 5.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  173 KSAKDaLLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD 252
Cdd:cd21198     1 SSGQD-LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78
                          90       100
                  ....*....|....*....|....*..
gi 117938332  253 PED-ISVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21198    79 PADmVLLSVPDKLSVMTYLHQIRAHFT 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
173-279 9.23e-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  Cd Length: 109  Bit Score: 117.77  E-value: 9.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   173 KSAKDALLLWCQMKTAGY-PNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHY--NLQNAFNLAEQHLGLTK 249
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 117938332   250 -LLDPEDIsvDHPDEKSIITYVVTYYHYFSK 279
Cdd:pfam00307   81 vLIEPEDL--VEGDNKSVLTYLASLFRRFQA 109
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
55-159 8.95e-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: 8.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLKEQRVHLENM 133
Cdd:cd21227     4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKpLNQHQKLENVTLALKAMAEDGIKLVNI 83
                          90       100
                  ....*....|....*....|....*.
gi 117938332  134 GSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21227    84 GNEDIVNGNLKLILGLIWHLILRYQI 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1063-1273 2.52e-29

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 117.55  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1063 KLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGE-MVTQGQTDAQYmfLR 1141
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEqLIEEGHPDAEE--IQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1142 QRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDAN 1221
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117938332 1222 EEKINAVVETGRRLVSDGNINSDR-IQEKVDSIDDRHRKNREAASELLMRLKD 1273
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEE 211
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
51-161 3.15e-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: 110.75  E-value: 3.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNSHLARVS--CRITDLYTDLRDGRMLIKLLEVLSGERLPKPTK-GRMRIHCLENVDKALQFLKEQR 127
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKpSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 117938332  128 VHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQD 161
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
174-277 5.09e-28

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: 110.14  E-value: 5.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21199     8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTI 86
                          90       100
                  ....*....|....*....|....*
gi 117938332  254 ED-ISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21199    87 DEmVSMERPDWQSVMSYVTAIYKHF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1699-1909 1.30e-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: 112.54  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1699 RLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQERVDTVNNMADELINSGHSDAATIAE 1778
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAH-EERVEALNELGEQLIEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1779 WKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKL-PEELGRDQNTVETLQRMHTTFEHDIQALG 1857
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALaSEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 117938332 1858 TQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRLVD 1909
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
177-277 1.62e-27

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: 108.32  E-value: 1.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  177 DALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI 256
Cdd:cd21226     3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                          90       100
                  ....*....|....*....|.
gi 117938332  257 SVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21226    83 MTGNPDERSIVLYTSLFYHAF 103
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
55-159 2.17e-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: 108.69  E-value: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLK-EQRVHLEN 132
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRpTFRSQKLENVSVALKFLEeDEGIKIVN 94
                          90       100
                  ....*....|....*....|....*..
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21311    95 IDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
174-274 6.11e-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: 107.00  E-value: 6.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|..
gi 117938332  254 ED-ISVDHPDEKSIITYVVTYY 274
Cdd:cd21259    81 EDmVRMREPDWKCVYTYIQEFY 102
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
179-277 7.36e-27

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: 106.66  E-value: 7.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-S 257
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMaS 88
                          90       100
                  ....*....|....*....|
gi 117938332  258 VDHPDEKSIITYVVTYYHYF 277
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELF 108
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
55-157 1.48e-26

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: 106.03  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKP--TKGRMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21183     4 IQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSynRRPAFQQHYLENVSTALKFIEADHIKLVN 83
                          90       100
                  ....*....|....*....|....*
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRF 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 2.59e-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: 104.87  E-value: 2.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                          90
                  ....*....|....*...
gi 117938332  254 EDISVDH-PDEKSIITYV 270
Cdd:cd21255    80 ADMVLLPiPDKLIVMTYL 97
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
55-157 3.66e-26

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: 104.88  E-value: 3.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRptFRQMKLENVSVALEFLERESIKLVS 83
                          90       100
                  ....*....|....*....|....*
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRF 157
Cdd:cd21228    84 IDSSAIVDGNLKLILGLIWTLILHY 108
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
179-277 4.34e-26

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: 104.64  E-value: 4.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-S 257
Cdd:cd21251    10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMaS 89
                          90       100
                  ....*....|....*....|
gi 117938332  258 VDHPDEKSIITYVVTYYHYF 277
Cdd:cd21251    90 VGEPDKLSMVMYLTQFYEMF 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1912-2075 6.32e-26

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 107.92  E-value: 6.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1912 DKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEK 1991
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1992 LLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDE 2071
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                  ....
gi 117938332 2072 RFSA 2075
Cdd:cd00176   161 RLKS 164
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
174-278 9.38e-26

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: 103.39  E-value: 9.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEqHLGLTKLLDP 253
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
                          90       100
                  ....*....|....*....|....*.
gi 117938332  254 EDISV-DHPDEKSIITYVVTYYHYFS 278
Cdd:cd21254    80 SDMVLlAVPDKLTVMTYLYQIRAHFS 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
638-742 1.27e-25

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 characteristic 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: 103.17  E-value: 1.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   638 RRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRE 717
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332   718 RIIYIREQWANLEQLSAIRKKRLEE 742
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
179-279 3.46e-25

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: 101.88  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  179 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD-PEDIS 257
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|..
gi 117938332  258 VDHPDEKSIITYVVTYYHYFSK 279
Cdd:cd21250    89 AEEPDKLSMVMYLSKFYELFRG 110
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
172-278 4.54e-25

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: 101.41  E-value: 4.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  172 KKSAKDALLLWCQMKTAGYpNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 251
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLL 79
                          90       100
                  ....*....|....*....|....*..
gi 117938332  252 DPEDISVDHPDEKSIITYVVTYYHYFS 278
Cdd:cd21245    80 EPEDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
176-274 1.07e-24

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: 100.93  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  176 KDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPED 255
Cdd:cd21260     3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                          90       100
                  ....*....|....*....|
gi 117938332  256 -ISVDHPDEKSIITYVVTYY 274
Cdd:cd21260    83 mVRMSVPDSKCVYTYIQELY 102
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
174-279 1.18e-24

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: 100.51  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90       100
                  ....*....|....*....|....*...
gi 117938332  254 EDISV--DHPDEKSIITYVVTYYHYFSK 279
Cdd:cd21258    81 EDMMImgKKPDSKCVFTYVQSLYNHLRR 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
54-159 2.94e-24

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  Cd Length: 109  Bit Score: 99.28  E-value: 2.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    54 AVQKKTFTKWVNSHLAR--VSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFL-KEQRVHL 130
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 117938332   131 ENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
174-277 9.18e-24

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: 97.73  E-value: 9.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90       100
                  ....*....|....*....|....*.
gi 117938332  254 EDISV--DHPDEKSIITYVVTYYHYF 277
Cdd:cd21261    81 EDMMVmgRKPDPMCVFTYVQSLYNHL 106
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
174-277 1.41e-23

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: 97.41  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21257     8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
                          90       100
                  ....*....|....*....|....*
gi 117938332  254 ED-ISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21257    87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
174-276 2.64e-23

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: 96.54  E-value: 2.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21184     1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
                          90       100
                  ....*....|....*....|....
gi 117938332  253 PEDISVDHPDEKSIITYVVTYYHY 276
Cdd:cd21184    78 PEDMVSPNVDELSVMTYLSYFRNA 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
177-271 3.37e-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: 95.85  E-value: 3.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    177 DALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKS----NAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80
                            90
                    ....*....|....*....
gi 117938332    253 PEDISVDHPDEKSIITYVV 271
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLI 99
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
55-159 9.87e-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: 95.48  E-value: 9.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   55 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERL-----PKPTKGRMRihcLENVDKALQFLKEQRVH 129
Cdd:cd21310    16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkyhPRPNFRQMK---LENVSVALEFLDREHIK 92
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332  130 LENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21310    93 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
58-156 1.13e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 94.69  E-value: 1.13e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332     58 KTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLPK--PTKGRMRIHCLENVDKALQFLKEQRVHLENMG 134
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 117938332    135 SHDIVDGNHrLTLGLIWTIILR 156
Cdd:smart00033   81 PEDLVEGPK-LILGVIWTLISL 101
SPEC smart00150
Spectrin repeats;
641-741 2.36e-22

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 93.55  E-value: 2.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    641 WKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERII 720
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    721 YIREQWANLEQLSAIRKKRLE 741
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
56-157 4.01e-22

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: 93.03  E-value: 4.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNSHLARVSCR--ITDLYTDLRDGRMLIKLLEVLSGERLPKP-TKGRMRIHCLENVDKALQFLKEQRVHLEN 132
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIhSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....*
gi 117938332  133 MGSHDIVDGNHRLTLGLIWTIILRF 157
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
2199-2307 1.08e-21

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: 92.78  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKHEWEAHNKKAS--SRSWHNVYCVINNQEMGFYKDAKSAASGIPYHS-EVPVSLKEAICEVALDYKKKKHVFK 2275
Cdd:cd13295     8 KKGYLMRKCCADPDGKKTPfgKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESlRNAISVHHSLATKATDYTKKPHVFR 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 117938332 2276 LRLSDGNEYLFQAKDDEEMNTWIQAI---SSAISS 2307
Cdd:cd13295    88 LRTADWREYLFQASDTKEMQSWIEAInlvAAAFSA 122
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
174-277 1.25e-21

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: 92.06  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 253
Cdd:cd21256    14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
                          90       100
                  ....*....|....*....|....*
gi 117938332  254 ED-ISVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21256    93 NEmVRTERPDWQSVMTYVTAIYKYF 117
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
2200-2303 9.43e-21

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: 89.35  E-value: 9.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2200 EGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPY--HSEVPVSLKEAICEVALDYKKKKHVFKLR 2277
Cdd:cd01253     3 EGWLHYKQIVTDKGKRVSDRSWKQAWAVLRGHSLYLYKDKREQTPALSIelGSEQRISIRGCIVDIAYSYTKRKHVFRLT 82
                          90       100
                  ....*....|....*....|....*.
gi 117938332 2278 LSDGNEYLFQAKDDEEMNTWIQAISS 2303
Cdd:cd01253    83 TSDFSEYLFQAEDRDDMLGWIKAIQE 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
53-159 3.98e-20

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: 88.21  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHL 130
Cdd:cd21309    15 KKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRptFRQMQLENVSVALEFLDRESIKL 94
                          90       100
                  ....*....|....*....|....*....
gi 117938332  131 ENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21309    95 VSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
53-153 2.71e-19

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: 85.28  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSC-RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFL-KEQRV 128
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKRGIpKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEpkNRIQMIQNLHLAMLFIeEDLKI 81
                          90       100
                  ....*....|....*....|....*
gi 117938332  129 HLENMGSHDIVDGNHRLTLGLIWTI 153
Cdd:cd21225    82 RVQGIGAEDFVDNNKKLILGLLWTL 106
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
53-159 3.25e-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: 85.52  E-value: 3.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   53 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHL 130
Cdd:cd21308    18 KKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRptFRQMQLENVSVALEFLDRESIKL 97
                          90       100
                  ....*....|....*....|....*....
gi 117938332  131 ENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21308    98 VSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
172-274 4.12e-19

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: 84.36  E-value: 4.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  172 KKSAKDALLLWCQmktAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKL 250
Cdd:cd21229     1 KIPPKKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMV 77
                          90       100
                  ....*....|....*....|....
gi 117938332  251 LDPEDISVDHPDEKSIITYvVTYY 274
Cdd:cd21229    78 LSPEDLSSPHLDELSGMTY-LSYF 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1592-1696 5.40e-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 characteristic 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: 84.29  E-value: 5.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1592 HKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISM 1671
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332  1672 RQSKVDKLYAGLKDLAEERRGKLDE 1696
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
849-952 5.95e-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 characteristic 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: 83.91  E-value: 5.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   849 LALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRA 928
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 117938332   929 QQDKLNTRWSQFRELVDRKKDALL 952
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2199-2306 6.47e-19

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  Cd Length: 102  Bit Score: 83.75  E-value: 6.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   2199 MEGFLNRKheweahnKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSevpVSLKEAICEVALDYK--KKKHVFKL 2276
Cdd:smart00233    3 KEGWLYKK-------SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGS---IDLSGCTVREAPDPDssKKPHCFEI 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 117938332   2277 RLSDGNEYLFQAKDDEEMNTWIQAISSAIS 2306
Cdd:smart00233   73 KTSDRKTLLLQAESEEEREKWVEALRKAIA 102
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
2200-2301 8.97e-19

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


Pssm-ID: 434701  Cd Length: 118  Bit Score: 84.02  E-value: 8.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  2200 EGFLNRKHEWEAHNKKASS--RSWHNVYCVINNQEMGFYKDAKSAASgipYHSEVPVSLKEA----------ICEVALDY 2267
Cdd:pfam15410    3 KGIVMRKCCFESKGKKTPRgkRSWKMVYAVLKDLVLYLYKDEHPPES---SQFEDKKSLKNApvgkirlhhaLATPAPDY 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 117938332  2268 KKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAI 2301
Cdd:pfam15410   80 TKKSHVFRLQTADGAEYLFQTGSPKELQEWVDTL 113
SPEC smart00150
Spectrin repeats;
1595-1695 3.21e-18

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 81.99  E-value: 3.21e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1595 QQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQS 1674
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332   1675 KVDKLYAGLKDLAEERRGKLD 1695
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1698-1801 3.56e-18

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 characteristic 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: 81.98  E-value: 3.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1698 HRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQERVDTVNNMADELINSGHSDAATIA 1777
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAH-QDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....
gi 117938332  1778 EWKDGLNEAWADLLELIDTRTQIL 1801
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1485-1590 4.00e-18

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 characteristic 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: 81.60  E-value: 4.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1485 KEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIItDSSSLNAEAIR 1564
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 117938332  1565 QRLADLKQLWGLLIEETEKRHRRLEE 1590
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
745-847 4.08e-18

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 characteristic 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: 81.60  E-value: 4.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   745 LLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQA-HAESPDVKGR 823
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEgHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 117938332   824 LAGIEERCKEMAELTRLRKQALQD 847
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
57-155 6.42e-18

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


Pssm-ID: 409031  Cd Length: 103  Bit Score: 80.85  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   57 KKTFTKWVNSHLA-RVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKP-TKGRMRIHCLENVDKALQFLKEQRVH-LENM 133
Cdd:cd00014     1 EEELLKWINEVLGeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInKKPKSPFKKRENINLFLNACKKLGLPeLDLF 80
                          90       100
                  ....*....|....*....|...
gi 117938332  134 GSHDIV-DGNHRLTLGLIWTIIL 155
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALAL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
530-636 7.75e-18

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 characteristic 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: 80.83  E-value: 7.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   530 LQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGegykPCDPQVI 609
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG----HYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 117938332   610 RDRVAHMEFCYQELCQLAAERRARLEE 636
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1914-2014 7.75e-18

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 characteristic 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: 80.83  E-value: 7.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1914 FRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLL 1993
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 117938332  1994 QLTEKRKEMIDKWEDRWEWLR 2014
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
1488-1589 1.11e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 80.45  E-value: 1.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1488 HQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIItDSSSLNAEAIRQRL 1567
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 117938332   1568 ADLKQLWGLLIEETEKRHRRLE 1589
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
422-525 1.65e-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 characteristic 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: 80.06  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   422 QLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITA 501
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90       100
                   ....*....|....*....|....
gi 117938332   502 RKDNVIRLWEYLLELLRARRQRLE 525
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
425-525 2.92e-17

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 78.91  E-value: 2.92e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    425 RRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKD 504
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    505 NVIRLWEYLLELLRARRQRLE 525
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2199-2306 5.73e-17

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 78.37  E-value: 5.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  2199 MEGFLNRKHEWEAhnkkassRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSevpVSLKEAICE--VALDYKKKKHVFKL 2276
Cdd:pfam00169    3 KEGWLLKKGGGKK-------KSWKKRYFVLFDGSLLYYKDDKSKKSKEPKGS---ISLSGCEVVevVASDSPKRKFCFEL 72
                           90       100       110
                   ....*....|....*....|....*....|...
gi 117938332  2277 RLSD---GNEYLFQAKDDEEMNTWIQAISSAIS 2306
Cdd:pfam00169   73 RTGErtgKRTYLLQAESEEERKDWIKAIQSAIR 105
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
174-281 1.14e-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: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 252
Cdd:cd21230     1 TPKQRLLGWIQNKI---PQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90       100
                  ....*....|....*....|....*....
gi 117938332  253 PEDISVDHPDEKSiityVVTYYHYFSKMK 281
Cdd:cd21230    78 PEEIINPNVDEMS----VMTYLSQFPKAK 102
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
2200-2307 1.41e-16

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: 77.32  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2200 EGFLNRKHEWEAHNKKasSRSWHNVYCVINNQEMGFYKDAKSAAsGIPYHSEVP---VSLKEAICEVALDYKKKKHVFKL 2276
Cdd:cd13233     3 QGLLNKTKIAENGKKL--RKNWSTSWVVLTSSHLLFYKDAKSAA-KSGNPYSKPessVDLRGASIEWAKEKSSRKNVFQI 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 117938332 2277 RLSDGNEYLFQAKDDEEMNTWIQAISSAISS 2307
Cdd:cd13233    80 STVTGTEFLLQSDNDTEIREWFDAIKAVIQR 110
SPEC smart00150
Spectrin repeats;
852-951 2.32e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 76.60  E-value: 2.32e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    852 YKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQD 931
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 117938332    932 KLNTRWSQFRELVDRKKDAL 951
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
176-275 2.39e-16

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  Cd Length: 103  Bit Score: 76.61  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  176 KDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHY---NLQNAFNLAEQH-LGLTKLL 251
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKkreNINLFLNACKKLgLPELDLF 80
                          90       100
                  ....*....|....*....|....
gi 117938332  252 DPEDIsVDHPDEKSIITYVVTYYH 275
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
56-150 2.58e-16

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 76.57  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNSHLA-RVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLP----KP-TKGRMRihclENVDKALQFLKEQRV 128
Cdd:cd21213     1 QLQAYVAWVNSQLKkRPGIRpVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPtTDAERK----ENVEKVLQFMASKRI 76
                          90       100
                  ....*....|....*....|..
gi 117938332  129 HLENMGSHDIVDGNHRLTLGLI 150
Cdd:cd21213    77 RMHQTSAKDIVDGNLKAIMRLI 98
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
957-1060 3.50e-16

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 characteristic 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: 76.20  E-value: 3.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   957 IQNYHLECNETKSWIREKTKVIEStQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSR 1036
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 117938332  1037 LAEISDVWEEMKTTLKNREASLGE 1060
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1065-1165 3.77e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.83  E-value: 3.77e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1065 QQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGE-MVTQGQTDAQYmfLRQR 1143
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEqLIEEGHPDAEE--IEER 78
                            90       100
                    ....*....|....*....|..
gi 117938332   1144 LQALDTGWNELHKMWENRQNLL 1165
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
1702-1801 4.40e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.83  E-value: 4.40e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1702 QLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIgQERVDTVNNMADELINSGHSDAATIAEWKD 1781
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAH-EERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 117938332   1782 GLNEAWADLLELIDTRTQIL 1801
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
1172-1272 7.16e-16

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 75.06  E-value: 7.16e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1172 QQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVD 1251
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332   1252 SIDDRHRKNREAASELLMRLK 1272
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1805-1909 9.92e-16

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 characteristic 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: 74.66  E-value: 9.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1805 YELHKFYHDAKEIFGRIQDKHKKL-PEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAyAGDKADDIQ 1883
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLsSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 117938332  1884 KRENEVLEAWKSLLDACEGRRVRLVD 1909
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
49-159 1.44e-15

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: 74.63  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   49 ADEREavqKKTFTKWVNSHLarVSCRITDLYTDLRDGRMLIKLLE-----VLSGERLPKPTKgRMRIHCLENVDKALQFL 123
Cdd:cd21219     1 EGSRE---ERAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKP-LNKFKKVENCNYAVDLA 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  124 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIlRFQI 159
Cdd:cd21219    75 KKLGFSLVGIGGKDIADGNRKLTLALVWQLM-RYHV 109
SPEC smart00150
Spectrin repeats;
531-635 2.49e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.52  E-value: 2.49e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    531 QKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGegykPCDPQVIR 610
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG----HPDAEEIE 76
                            90       100
                    ....*....|....*....|....*
gi 117938332    611 DRVAHMEFCYQELCQLAAERRARLE 635
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1915-2013 3.17e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 3.17e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1915 RFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLLQ 1994
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 117938332   1995 LTEKRKEMIDKWEDRWEWL 2013
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
747-846 3.53e-15

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 73.13  E-value: 3.53e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    747 HQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQA-HAESPDVKGRLA 825
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEgHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 117938332    826 GIEERCKEMAELTRLRKQALQ 846
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
174-277 4.71e-15

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


Pssm-ID: 409045  Cd Length: 106  Bit Score: 73.16  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  174 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 253
Cdd:cd21196     3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                          90       100
                  ....*....|....*....|....
gi 117938332  254 EDIsVDHPDEKSIITYVVTYYHYF 277
Cdd:cd21196    83 QAV-VAGSDPLGLIAYLSHFHSAF 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1380-1483 4.98e-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 characteristic 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: 4.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1380 NKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGK-STDEVDS 1458
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHyASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332  1459 KRLTVQTKFMELLEPLSERKHNLLA 1483
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1275-1378 2.98e-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 characteristic 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: 70.81  E-value: 2.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1275 RDLQKFLQDCQELSLWINEKM--LTAQDMSYD--EARNLHSKwlkHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAV 1350
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEalLSSEDYGKDleSVQALLKK---HKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 117938332  1351 VKEKLTGLHKMWEVLESTTQTKAQRLFD 1378
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1063-1167 3.10e-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 characteristic 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: 70.43  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1063 KLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQyMFLRQ 1142
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 117938332  1143 RLQALDTGWNELHKMWENRQNLLSQ 1167
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
958-1058 6.80e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 6.80e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332    958 QNYHLECNETKSWIREKTKVIESTqDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRL 1037
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 117938332   1038 AEISDVWEEMKTTLKNREASL 1058
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
51-159 1.27e-13

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: 69.37  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAvqkKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLE-VLSGE------RLPKPTKGRMRIHCLENVDKALQFL 123
Cdd:cd21300     6 EREA---RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvNKAPASAEISRFKAVENTNYAVELG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  124 KEQRVHLENMGSHDIVDGNHRLTLGLIWTiILRFQI 159
Cdd:cd21300    81 KQLGFSLVGIQGADITDGSRTLTLALVWQ-LMRFHI 115
SPEC smart00150
Spectrin repeats;
1278-1376 1.44e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.51  E-value: 1.44e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1278 QKFLQDCQELSLWINEKMLTAQDMSY-DEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLT 1356
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|
gi 117938332   1357 GLHKMWEVLESTTQTKAQRL 1376
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
51-160 1.67e-13

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 68.80  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLE------VLSGERLPKPTKGRMRIHCLENVDKALQFLK 124
Cdd:cd21298     2 IEETREEKTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDkikpgvVDWSRVNKPFKKLGANMKKIENCNYAVELGK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  125 EQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQ 160
Cdd:cd21298    80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
74-154 2.15e-13

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: 68.39  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   74 RITDLYTDLRDGRMLIKLLEVLSGERLPK-----PTKGRMR-IHcleNVDKALQFLKEQRVHLENMGSH----DIVDGNH 143
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLsklrvPAISRLQkLH---NVEVALKALKEAGVLRGGDGGGitakDIVDGHR 101
                          90
                  ....*....|.
gi 117938332  144 RLTLGLIWTII 154
Cdd:cd21223   102 EKTLALLWRII 112
SPEC smart00150
Spectrin repeats;
1808-1907 3.56e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 67.35  E-value: 3.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1808 HKFYHDAKEIFGRIQDKHKKL-PEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDkADDIQKRE 1886
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLaSEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 117938332   1887 NEVLEAWKSLLDACEGRRVRL 1907
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
165-273 4.62e-13

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: 67.88  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  165 ETEDNKEKKSAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQ 243
Cdd:cd21315     7 DGPDDGKGPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAED 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332  244 HLGLTKLLDPEDISVDHPDEKSIITYVVTY 273
Cdd:cd21315    84 WLDVPQLIKPEEMVNPKVDELSMMTYLSQF 113
SPEC smart00150
Spectrin repeats;
1385-1481 7.31e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.58  E-value: 7.31e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   1385 FTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEG-KSTDEVDSKRLTV 1463
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGhPDAEEIEERLEEL 82
                            90
                    ....*....|....*...
gi 117938332   1464 QTKFMELLEPLSERKHNL 1481
Cdd:smart00150   83 NERWEELKELAEERRQKL 100
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
165-273 3.62e-11

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: 62.40  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  165 ETEDNKEKKSAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQ 243
Cdd:cd21314     2 EDEEDARKQTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADD 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332  244 HLGLTKLLDPEDISVDHPDEKSIITYVVTY 273
Cdd:cd21314    79 WLGVPQVIAPEEIVDPNVDEHSVMTYLSQF 108
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
2199-2301 1.17e-10

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: 59.86  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKHEWeahnkkaSSRSWHNVYCVINNQEMGFYKDaKSAASGIPYHSevpVSLKEAICEVALDYKKKKHVFKLRL 2278
Cdd:cd00821     1 KEGYLLKRGGG-------GLKSWKKRWFVLFEGVLLYYKS-KKDSSYKPKGS---IPLSGILEVEEVSPKERPHCFELVT 69
                          90       100
                  ....*....|....*....|...
gi 117938332 2279 SDGNEYLFQAKDDEEMNTWIQAI 2301
Cdd:cd00821    70 PDGRTYYLQADSEEERQEWLKAL 92
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
58-153 3.94e-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: 58.89  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   58 KTFTKWVNSHLARVSCR--ITDLYTDLRDGRMLIKLLEVLSGERL------PKpTKGRMrihcLENVDKALQFLKEQRVH 129
Cdd:cd21286     3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVedingcPR-SQSQM----IENVDVCLSFLAARGVN 77
                          90       100
                  ....*....|....*....|....
gi 117938332  130 LENMGSHDIVDGNHRLTLGLIWTI 153
Cdd:cd21286    78 VQGLSAEEIRNGNLKAILGLFFSL 101
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
165-273 2.19e-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: 57.12  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  165 ETEDNKEKKSAKDALLLWCQMKtagYPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQ 243
Cdd:cd21312     3 EEDEEAKKQTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332  244 HLGLTKLLDPEDISVDHPDEKSIITYVVTY 273
Cdd:cd21312    80 WLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
166-273 2.40e-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: 57.02  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  166 TEDNKeKKSAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQH 244
Cdd:cd21313     1 DDDAK-KQTPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDW 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 117938332  245 LGLTKLLDPEDISvdHP--DEKSIITYVVTY 273
Cdd:cd21313    77 LGVPQVITPEEII--HPdvDEHSVMTYLSQF 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
57-154 3.59e-09

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  Cd Length: 114  Bit Score: 56.43  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   57 KKTFTKWVNSHLAR---VSCRIT------DLYTDLRDGRMLIKLLE-------VLSGERLPKPtkgrMRIH-CLENVDKA 119
Cdd:cd21217     3 KEAFVEHINSLLADdpdLKHLLPidpdgdDLFEALRDGVLLCKLINkivpgtiDERKLNKKKP----KNIFeATENLNLA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 117938332  120 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 154
Cdd:cd21217    79 LNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
177-270 8.13e-09

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


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 56.16  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  177 DALLLWCQMKTAGYpNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLK------------------------------ 226
Cdd:cd21224     3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRqpttqtvdraqdeaedfwvaefspstgdsg 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 117938332  227 -----KSNAHYNLQnAFNLAEQHLG-LTKLLDPEDISVDHPDEKSIITYV 270
Cdd:cd21224    82 lsselLANEKRNFK-LVQQAVAELGgVPALLRASDMSNTIPDEKVVILFL 130
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
51-159 9.69e-09

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: 55.78  E-value: 9.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 124
Cdd:cd21331    18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVELGK 95
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  125 EQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21331    96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1169-1266 3.55e-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 characteristic 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: 53.48  E-value: 3.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1169 HAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQE 1248
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
                           90
                   ....*....|....*...
gi 117938332  1249 KVDSIDDRHRKNREAASE 1266
Cdd:pfam00435   81 RLEELNERWEQLLELAAE 98
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
2201-2307 4.49e-08

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn 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: 269937  Cd Length: 127  Bit Score: 53.62  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2201 GFLNRKHeWEAHNKK-----ASSRSWHNVYCVINNQEMGFYK-DAKSAAS--GIPYHS-EVPVSLKEAICEvaldYKKKK 2271
Cdd:cd01230     7 GWLSVKN-FLVHKKNkkvelATRRKWKKYWVCLKGCTLLFYEcDERSGIDenSEPKHAlFVEGSIVQAVPE----HPKKD 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332 2272 HVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSAISS 2307
Cdd:cd01230    82 FVFCLSNSFGDAYLFQATSQTELENWVTAIHSACAS 117
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
302-412 4.76e-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 characteristic 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: 4.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   302 KMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAfntYRTVEKPPKfTEKGNLEVLLfTIQSKMrANNQKVY 381
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELA-AHQDRVEALN-ELAEKL-IDEGHYA 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 117938332   382 MPREGKLISDINKAWERLEKAEHERELALRN 412
Cdd:pfam00435   75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
791-1718 7.62e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.19  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  791 EEITNYRPT-IDTLHEQASALPQAHAESPDVKGRLAGIEERCKE--------MAELTRLRKQA--LQDTLALYKMFSEAD 859
Cdd:COG1196   147 EEIINAKPEeRRKLIEEAAGVSKYKERKEEAERKLERTEENLERledlleelEKQLEKLERQAekAERYQELKAELRELE 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  860 ACELWIDEKEqwlNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQiarqlmhnghpSEKEIRAQQDKLNTRWSQ 939
Cdd:COG1196   227 LALLLAKLKE---LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKS-----------ELEELREELEELQEELLE 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  940 FR-ELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIEST-QDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQK 1017
Cdd:COG1196   293 LKeEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALkEELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1018 EAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGE-ASKLQQFLRDLDDFQSWLSRTQTAIASEDmpntlTE 1096
Cdd:COG1196   373 ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERlSERLEDLKEELKELEAELEELQTELEELN-----EE 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1097 AEKLLTQHENIKNEIDNYEEDYQKMRDmgemvtqgqtdAQYMfLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLR 1176
Cdd:COG1196   448 LEELEEQLEELRDRLKELERELAELQE-----------ELQR-LEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1177 DTKQAEAFLN--NQEYVLAhtempttlegAEAAIKKQEDFM--TTMDANEEKINAVVETGRRLVSDgnINSDRIQEKVDS 1252
Cdd:COG1196   516 GVYGPVAELIkvKEKYETA----------LEAALGNRLQAVvvENEEVAKKAIEFLKENKAGRATF--LPLDRIKPLRSL 583
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1253 IDDRHRKNREAASELLmrlkdnrdlqKFLQDCQELSLWINEKMLTAQDMsyDEARNLHSKwLKHQAFMAELASnkewlDK 1332
Cdd:COG1196   584 KSDAAPGFLGLASDLI----------DFDPKYEPAVRFVLGDTLVVDDL--EQARRLARK-LRIKYRIVTLDG-----DL 645
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1333 IEKEG-MQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKA-ELFTQSCADLDKWLHGLESQIQSDDygk 1410
Cdd:COG1196   646 VEPSGsITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNElRSLEDLLEELRRQLEELERQLEELK--- 722
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1411 dlTSVNILLKKQQMLENQMEVRKKEIEELQSQaqalsqEGKSTDEVDSKRLTVQTKFMELLEPLSERKHNLLASKEIHQF 1490
Cdd:COG1196   723 --RELAALEEELEQLQSRLEELEEELEELEEE------LEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE 794
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1491 NRDVEDEILWVGERMpLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDdifersqniitdSSSLNAEAIRQRLADL 1570
Cdd:COG1196   795 LEELEEELEEAERRL-DALERELESLEQRRERLEQEIEELEEEIEELEEKLD------------ELEEELEELEKELEEL 861
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1571 KQLwgllIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILE-QAVEDYAETVH 1649
Cdd:COG1196   862 KEE----LEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEvELPELEEELEE 937
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117938332 1650 QLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRlfQLNREVDDLEQWIAERE 1718
Cdd:COG1196   938 EYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRE--DLEEAKEKLLEVIEELD 1004
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
189-258 7.85e-08

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 51.53  E-value: 7.85e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117938332   189 GYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDK--LKK--SNAH--YNLQNAFNLAEQHLGLTKL-LDPEDISV 258
Cdd:pfam11971    7 LPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDicLKEsmSLADslYNIQLLQEFCQRHLGNRCChLTLEDLLY 83
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
54-153 7.95e-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: 53.04  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   54 AVQKKTFTKWVNSHLARVSCR--ITDLYTDLRDGRMLIKLLEVLSGERL------PKPtkgrmRIHCLENVDKALQFLKE 125
Cdd:cd21285     9 GFDKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIedingcPKN-----RSQMIENIDACLSFLAA 83
                          90       100
                  ....*....|....*....|....*...
gi 117938332  126 QRVHLENMGSHDIVDGNHRLTLGLIWTI 153
Cdd:cd21285    84 KGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
51-159 8.03e-08

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: 53.07  E-value: 8.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 124
Cdd:cd21330     9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLgeNMKKLENCNYAVELGK 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  125 EQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21330    87 NKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2017-2075 8.95e-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 characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 8.95e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 117938332  2017 LEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSA 2075
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEA 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
993-1287 1.09e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   993 ALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKttlknreaSLGEASKLQqFLRDLD 1072
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--------DLGEEEQLR-VKEKIG 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1073 DFQSWLSRTQTAIAS-----EDMPNTLTEAE----KLLTQHENIKNEIdnyeEDYQKMRD-MGEMVTQGQtdAQYMFLRQ 1142
Cdd:TIGR02169  298 ELEAEIASLERSIAEkerelEDAEERLAKLEaeidKLLAEIEELEREI----EEERKRRDkLTEEYAELK--EELEDLRA 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1143 RLQALDTG---WNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAflnnQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMD 1219
Cdd:TIGR02169  372 ELEEVDKEfaeTRDELKDYREKLEKLKREINELKRELDRLQEEL----QRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117938332  1220 ANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQEL 1287
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
62-153 1.09e-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: 52.30  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   62 KWVNSHLARV---SCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRM--RIHCLENVDKALQFLKE--QRVHLEnmg 134
Cdd:cd21218    17 RWVNYHLKKAgptKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlsEEDLEKRAEKVLQAAEKlgCKYFLT--- 93
                          90
                  ....*....|....*....
gi 117938332  135 SHDIVDGNHRLTLGLIWTI 153
Cdd:cd21218    94 PEDIVSGNPRLNLAFVATL 112
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
56-159 1.30e-07

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: 52.12  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLE-----VLSGERLPKPTKgRMRIHCLENVDKALQFLKEQRVHL 130
Cdd:cd21299     5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPI-KMPFKKVENCNQVVKIGKQLKFSL 81
                          90       100
                  ....*....|....*....|....*....
gi 117938332  131 ENMGSHDIVDGNHRLTLGLIWTiILRFQI 159
Cdd:cd21299    82 VNVAGNDIVQGNKKLILALLWQ-LMRYHM 109
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
51-159 1.52e-07

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: 51.91  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   51 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLEV----LSGERLPKPT----KGRMRIhcLENVDKALQF 122
Cdd:cd21329     2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpVDWGHVNKPPypalGGNMKK--IENCNYAVEL 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 117938332  123 LKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILRFQI 159
Cdd:cd21329    78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
SPEC smart00150
Spectrin repeats;
2020-2075 2.00e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.18  E-value: 2.00e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 117938332   2020 HQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSA 2075
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEA 56
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
789-1590 2.17e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 56.65  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  789 VAEEITNYRPTIDTLHEQASALPQAHAE-SPDVKGRLAGIEERCKEMAELTRLRKQALQDTLALYKMfseadacelwIDE 867
Cdd:COG1196   230 LLAKLKELRKELEELEEELSRLEEELEElQEELEEAEKEIEELKSELEELREELEELQEELLELKEE----------IEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  868 KEQWLNNM--QIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNghpsEKEIRAQQDKLNTRWSQFRELVD 945
Cdd:COG1196   300 LEGEISLLreRLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQL----LAELEEAKEELEEKLSALLEELE 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  946 RKKDALLSALSIQNYHLECNETKswIREKTKVIESTQDLGNDLAgvmalqRKLTGMERDLVAIEAKLSDLQKEAEKLESE 1025
Cdd:COG1196   376 ELFEALREELAELEAELAEIRNE--LEELKREIESLEERLERLS------ERLEDLKEELKELEAELEELQTELEELNEE 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1026 hpdqaqailsrLAEISDVWEEMKTTLKNREASLGEA-SKLQQFLRDLDDFQSWLSRTQTAiaSEDMPNTLTEAEKLLTQH 1104
Cdd:COG1196   448 -----------LEELEEQLEELRDRLKELERELAELqEELQRLEKELSSLEARLDRLEAE--QRASQGVRAVLEALESGL 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1105 ENIKN---EIDNYEEDYQKM------RDMGEMVTQGQTDAQ--YMFLRQRLQALDTgWNELHKMwenRQNLLSQSHAYQQ 1173
Cdd:COG1196   515 PGVYGpvaELIKVKEKYETAleaalgNRLQAVVVENEEVAKkaIEFLKENKAGRAT-FLPLDRI---KPLRSLKSDAAPG 590
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1174 FLR--------DTKQAEAFlnnqEYVLAHTEMPTTLEGAEAAIKKqedfmttmdaNEEKINAVVETGRRLVSDGNINS-- 1243
Cdd:COG1196   591 FLGlasdlidfDPKYEPAV----RFVLGDTLVVDDLEQARRLARK----------LRIKYRIVTLDGDLVEPSGSITGgs 656
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1244 -------------DRIQEKVDSIDDRHRKNREAASELlmrlkdNRDLQKFLQDCQELSLWINEKMLtAQDMSYDEARNLH 1310
Cdd:COG1196   657 rnkrsslaqkrelKELEEELAELEAQLEKLEEELKSL------KNELRSLEDLLEELRRQLEELER-QLEELKRELAALE 729
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1311 SKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELftqsca 1390
Cdd:COG1196   730 EELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELE------ 803
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1391 DLDKWLHGLESQIQSddygkdltsvniLLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKStdevdskrltVQTKFMEL 1470
Cdd:COG1196   804 EAERRLDALERELES------------LEQRRERLEQEIEELEEEIEELEEKLDELEEELEE----------LEKELEEL 861
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1471 LEPLSERKHNLLASKEIHQFNRDVEDEilwVGERMPLATSTDHGHNLQTVQLLIKKNQT---LQKEIQGHQPRIDDIFER 1547
Cdd:COG1196   862 KEELEELEAEKEELEDELKELEEEKEE---LEEELRELESELAELKEEIEKLRERLEELeakLERLEVELPELEEELEEE 938
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|...
gi 117938332 1548 SQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEE 1590
Cdd:COG1196   939 YEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEE 981
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
49-157 3.66e-07

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: 51.05  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   49 ADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLP------KPTKGRMRIHcleNVDKALQF 122
Cdd:cd21222    10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyhlTPSTDDEKLH---NVKLALEL 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 117938332  123 LKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRF 157
Cdd:cd21222    87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
191-275 6.57e-07

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: 49.61  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  191 PNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDPEDISVDHPDEKSIITYV 270
Cdd:cd21185    15 PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYA 93

                  ....*
gi 117938332  271 VTYYH 275
Cdd:cd21185    94 AQLQK 98
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
56-156 1.14e-06

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: 49.75  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNSHLAR---VSCRI---TD---LYTDLRDGRMLIKLL--------EVLSGERLPKPTKGRMRIHCLENVDK 118
Cdd:cd21294     7 ERREFTKHINAVLAGdpdVGSRLpfpTDtfqLFDECKDGLVLSKLIndsvpdtiDERVLNKPPRKNKPLNNFQMIENNNI 86
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 117938332  119 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 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 ...
165-275 1.16e-06

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 49.22  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  165 ETEDNKEKKSAKDALLLWC--QMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKS--------NAHYNL 234
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVnyHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlseedlekRAEKVL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117938332  235 QNAfnlaeQHLGLTKLLDPEDISvdHPDEKSIITYVVTYYH 275
Cdd:cd21218    81 QAA-----EKLGCKYFLTPEDIV--SGNPRLNLAFVATLFN 114
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1108-1888 2.22e-05

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 50.10  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1108 KNEIDNYEEDY-QKMRDMGEMVTQGQT--DAQYMFLRQRLQALDTgwnELHKMWENRQnllsqshAYQQFLRDTKQAEAF 1184
Cdd:pfam15921   73 KEHIERVLEEYsHQVKDLQRRLNESNElhEKQKFYLRQSVIDLQT---KLQEMQMERD-------AMADIRRRESQSQED 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1185 LNNQeyvlahteMPTTLEGAEAAIKKQEDFMTTMDANEEKI-------NAVVETGRRLVSDGNINSDRIQEKVDSIDDRH 1257
Cdd:pfam15921  143 LRNQ--------LQNTVHELEAAKCLKEDMLNDSNTQIEQLrkmmlshEGVLQEIRSILVDFEEASGKKIYEHDSMSTIH 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1258 RKNREAASELLMRLKDNrdlqkflqdcqELSlWINEKMLTAQDmsydearnlhskwlKHQAFMAELASNKEWL-----DK 1332
Cdd:pfam15921  215 FRSLGSAISKILRELDT-----------EIS-YLKGRIFPVED--------------QLEALKSESQNKIELLlqqhqDR 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1333 IEkegmQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLfdANKAELFTQSCADLDKWLHGLESQIQSddygkdl 1412
Cdd:pfam15921  269 IE----QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA--RNQNSMYMRQLSDLESTVSQLRSELRE------- 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1413 tSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEvdskrltvqtKFMELLEPLSERKHNLLASKEIHQ--F 1490
Cdd:pfam15921  336 -AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD----------QLQKLLADLHKREKELSLEKEQNKrlW 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1491 NRDVEDEILWVGERMPLatsTDHGHNLQTVQLLIKknqTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEairqrLADL 1570
Cdd:pfam15921  405 DRDTGNSITIDHLRREL---DDRNMEVQRLEALLK---AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ-----LEST 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1571 KQLWGLLIEETEKRHRRLEEAHKA----------QQYYFDAAEAEAW-------MSEQELYMMSEE-------KAKDEQS 1626
Cdd:pfam15921  474 KEMLRKVVEELTAKKMTLESSERTvsdltaslqeKERAIEATNAEITklrsrvdLKLQELQHLKNEgdhlrnvQTECEAL 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1627 AVSMLKKHQILE---QAVEDYAETVHQLSKTSRAL-VADSHPESE----RISMRQSKV--DKLYAGLKDLaEERRGKLD- 1695
Cdd:pfam15921  554 KLQMAEKDKVIEilrQQIENMTQLVGQHGRTAGAMqVEKAQLEKEindrRLELQEFKIlkDKKDAKIREL-EARVSDLEl 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1696 ERHRLFQLN----REVDDLEQwiaEREVVAgsHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNNMADELiNSGHS 1771
Cdd:pfam15921  633 EKVKLVNAGserlRAVKDIKQ---ERDQLL--NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL-KSAQS 706
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1772 DAATI------AEWKDG--LNEAWADLLELIDTRTQILAASYELhKFYHDAkeIFGRIQDKHkKLPEELGRDQNTVETLQ 1843
Cdd:pfam15921  707 ELEQTrntlksMEGSDGhaMKVAMGMQKQITAKRGQIDALQSKI-QFLEEA--MTNANKEKH-FLKEEKNKLSQELSTVA 782
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|...
gi 117938332  1844 RMHTTFEHDIQALGTQVRQLQEDAARLQAAYagDKA--------DDIQKRENE 1888
Cdd:pfam15921  783 TEKNKMAGELEVLRSQERRLKEKVANMEVAL--DKAslqfaecqDIIQRQEQE 833
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1004-1710 2.36e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1004 DLVAIEAKLSDLQKEAEKLESEHpdqaQAILSRLAEISDVWEEMKTTLKNREASLGEA-SKLQQFLRDLDDFQSwlsrtQ 1082
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRLEVSELEEEIEELqKELYALANEISRLEQ-----Q 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1083 TAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMvtqgqtdaqymfLRQRLQALDtgwNELHKMWENRQ 1162
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE------------LKEELESLE---AELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1163 NLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHT--EMPTTLEGAEAAIKKQEDfmttmdANEEKINAVVETGRRLVSDGN 1240
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQ------EIEELLKKLEEAELKELQAEL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1241 INSDRIQEKVDSIDDRHRKNREAASELLMRLKdnRDLQKFLQDCQELSLWIN--EKMLTAQDMSYDEARNL-HSKWLKHQ 1317
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAE--QALDAAERELAQLQARLDslERLQENLEGFSEGVKALlKNQSGLSG 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1318 AF--MAELAS-NKEWLDKIEK---EGMQLI------SEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELF 1385
Cdd:TIGR02168  521 ILgvLSELISvDEGYEAAIEAalgGRLQAVvvenlnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1386 TQSCADLDK-----------WLHGL------------------ESQIQSDD-----------YGKDLTSVNILLKKQQM- 1424
Cdd:TIGR02168  601 LGVAKDLVKfdpklrkalsyLLGGVlvvddldnalelakklrpGYRIVTLDgdlvrpggvitGGSAKTNSSILERRREIe 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1425 -LENQMEVRKKEIEELQSQAQALSQEgksTDEVDSKRLTVQTKFMELLEPLSERKHNLLASKEIHQ----FNRDVEDEIL 1499
Cdd:TIGR02168  681 eLEEKIEELEEKIAELEKALAELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELT 757
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1500 WVGERMPLATSTDHGHNLQTVQLLIKKnQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEA--IRQRLADLKQ---LW 1574
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAanLRERLESLERriaAT 836
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1575 GLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQL--- 1651
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrre 916
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117938332  1652 SKTSRALVADSHPESERISMR----QSKVDKLYAGLKDLAEERRGKLDE-----RHRLFQLNREVDDL 1710
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKEL 984
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
2265-2305 2.69e-05

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain 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: 270113  Cd Length: 108  Bit Score: 45.06  E-value: 2.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 117938332 2265 LDYKKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSAI 2305
Cdd:cd13301    58 LEYGKRPLVFKLTTAKGQEHFFQACSREERDAWAKDITKAI 98
PH_DOCK-D cd13267
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ...
2217-2318 4.63e-05

Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. 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: 270087  Cd Length: 126  Bit Score: 45.01  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2217 SSRSWHNVYCVINNQEMG-----FYKDAKSAASgipyhsevpvslKEAIC-----EVALDYKKKKHVFKLRLSDGNEYLF 2286
Cdd:cd13267    27 AMKSFKRRFFHLKQLVDGsyileFYKDEKKKEA------------KGTIFldsctGVVQNSKRRKFCFELRMQDKKSYVL 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 117938332 2287 QAKDDEEMNTWIQAISSAISSDKHDTSASTQS 2318
Cdd:cd13267    95 AAESEAEMDEWISKLNKILQSSKEQSIQKKRS 126
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
57-143 5.07e-05

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: 44.19  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   57 KKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTK---GRMRIHCLENVDKALQFLkeqrVHLENM 133
Cdd:cd21221     3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVaqsEEGQKQKLAVVLACVNFL----LGLEED 78
                          90
                  ....*....|
gi 117938332  134 GSHDIVDGNH 143
Cdd:cd21221    79 EARWTVDGIY 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
924-1795 1.26e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   924 KEIRAQQDKLNTRWSQ---FRELVDRKKDALLSALsiqnyhlecneTKSWIREKTKVIESTQDLGndlagvmALQRKLTG 1000
Cdd:TIGR02168  196 NELERQLKSLERQAEKaerYKELKAELRELELALL-----------VLRLEELREELEELQEELK-------EAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1001 MERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVwEEMKTTLKNREASLgeASKLQQFLRDLDDFQSWLSR 1080
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-EQQKQILRERLANL--ERQLEELEAQLEELESKLDE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1081 TQTAIASEDmpntlTEAEKLLTQHENIKNEIDNYEEDYQKMrdmgemvtqgqtdaqymflRQRLQALDTGWNELHKMWEN 1160
Cdd:TIGR02168  335 LAEELAELE-----EKLEELKEELESLEAELEELEAELEEL-------------------ESRLEELEEQLETLRSKVAQ 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1161 RQNLLSQSHAYQQFLRDTKQAeaflnnqeyvLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVsdgn 1240
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLER----------LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL---- 456
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1241 insDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELslwinekmltAQDMSYDEARNLHSKWLKHQAF- 1319
Cdd:TIGR02168  457 ---ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----------LEGFSEGVKALLKNQSGLSGILg 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1320 -MAELAS-NKEWLDKIEK---EGMQLI------SEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQS 1388
Cdd:TIGR02168  524 vLSELISvDEGYEAAIEAalgGRLQAVvvenlnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1389 CADLDKWLHGLESQIQSDDYG----KDLTSVNILLKK-----------------------------QQMLENQMEVRK-- 1433
Cdd:TIGR02168  604 AKDLVKFDPKLRKALSYLLGGvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnSSILERRREIEEle 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1434 KEIEELQSQAQALSQEgkstdevdskRLTVQTKFMELLEPLSERKhnllasKEIHQFNRDVedeilwVGERMPLATSTDH 1513
Cdd:TIGR02168  684 EKIEELEEKIAELEKA----------LAELRKELEELEEELEQLR------KELEELSRQI------SALRKDLARLEAE 741
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1514 GHNL-QTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEAirQRLADLKQLWGLLIEETEKRHRRLEEAH 1592
Cdd:TIGR02168  742 VEQLeERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTLLNEEA 819
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1593 KAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSmlkkhqiLEQAVEDYAETVHQLSKTSRALVADSHPESERISMR 1672
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALL 892
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1673 QSKVDKLYAGLKDLAEER---RGKLDE-RHRLFQLNREVDDLEQWIAE-REVVAGSHEL-----GQDYEHVTMLQERFRE 1742
Cdd:TIGR02168  893 RSELEELSEELRELESKRselRRELEElREKLAQLELRLEGLEVRIDNlQERLSEEYSLtleeaEALENKIEDDEEEARR 972
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....
gi 117938332  1743 FARDTGN-IgqERVDTVNNMADELINSGHSDAATIAEWKDGLNEAWADLLELID 1795
Cdd:TIGR02168  973 RLKRLENkI--KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
49-157 1.42e-04

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: 43.56  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   49 ADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLP------KPTKGRMRIHcleNVDKALQF 122
Cdd:cd21306    10 APDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhsfhlTPTSFEQKVH---NVQFAFEL 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 117938332  123 LKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRF 157
Cdd:cd21306    87 MQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
46-158 1.58e-04

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  Cd Length: 122  Bit Score: 43.49  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   46 KALADEREAVqKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLP------KPTKGRMRIHcleNVDKA 119
Cdd:cd21307     8 KLGPDKVNTV-KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsefflTPSSTSEMLH---NVTLA 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 117938332  120 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQ 158
Cdd:cd21307    84 LELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
2199-2311 2.25e-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: 42.61  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKheweAHNKKassrSWHNVYCVINNQEMGFYKDAKSaasgipyHSEVPVSLKEAICEVA-LDYKKKKHVFKLR 2277
Cdd:cd13298     8 KSGYLLKR----SRKTK----NWKKRWVVLRPCQLSYYKDEKE-------YKLRRVINLSELLAVApLKDKKRKNVFGIY 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 117938332 2278 LSDGNeYLFQAKDDEEMNTWIQAISSAISSDKHD 2311
Cdd:cd13298    73 TPSKN-LHFRATSEKDANEWVEALREEFRLDDEE 105
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
49-158 3.69e-04

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


Pssm-ID: 409186  Cd Length: 129  Bit Score: 42.67  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   49 ADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLP------KPTKGRMRIHcleNVDKALQF 122
Cdd:cd21337    14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPlhsfflTPDSFEQKVL---NVSFAFEL 90
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 117938332  123 LKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQ 158
Cdd:cd21337    91 MQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
56-154 4.03e-04

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 42.65  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNSHLAR-VSCR--------ITDLYTDLRDGRMLIKLLEVLS----GER-LPKPTKGRMRIHclENVDKALQ 121
Cdd:cd21292    25 EKVAFVNWINKNLGDdPDCKhllpmdpnTDDLFEKVKDGILLCKMINLSVpdtiDERaINKKKLTVFTIH--ENLTLALN 102
                          90       100       110
                  ....*....|....*....|....*....|...
gi 117938332  122 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 154
Cdd:cd21292   103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
2214-2307 4.54e-04

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 41.99  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2214 KKASS--RSWHNVYCVINNQEMGFYKDAK-SAASG-IPYH----SEVPVSLKEAicevaldykkKKHVFKLRLSDGNE-- 2283
Cdd:cd13263    10 KKQGSivKNWQQRWFVLRGDQLYYYKDEDdTKPQGtIPLPgnkvKEVPFNPEEP----------GKFLFEIIPGGGGDrm 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332 2284 ------YLFQAKDDEEMNTWIQAISSAISS 2307
Cdd:cd13263    80 tsnhdsYLLMANSQAEMEEWVKVIRRVIGS 109
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
997-1449 5.92e-04

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 45.09  E-value: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   997 KLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLknREASLGEASKLQQFLRDLDDFQS 1076
Cdd:pfam15921  279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEL--REAKRMYEDKIEELEKQLVLANS 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1077 WLS--RTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKM--RDMGEMVT----QGQTDAQYMFLrQRLQALd 1148
Cdd:pfam15921  357 ELTeaRTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdRDTGNSITidhlRRELDDRNMEV-QRLEAL- 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1149 tgwneLHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQ---------EYVLAHTEMPTTLEGAEAAIkkqEDFMTTMD 1219
Cdd:pfam15921  435 -----LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQlestkemlrKVVEELTAKKMTLESSERTV---SDLTASLQ 506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1220 ANEEKINAVVETGRRLVSDGNINSDRIQE-KVDSIDDRHRKNREAASELLMRLKDnRDLQKFLQDCQELSLWINEKMLTA 1298
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHlKNEGDHLRNVQTECEALKLQMAEKD-KVIEILRQQIENMTQLVGQHGRTA 585
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1299 QDMSYDEA---RNLHSKWLKHQAFM-------AELASNKEWLDKIEKEGMQLISEKPETEAVVKE--------------- 1353
Cdd:pfam15921  586 GAMQVEKAqleKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqllnevkts 665
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332  1354 --KLTGLHKMWEVLESTTQTKAQRL-FDANKAELFTQSC-ADLDKWLHGLESQIQSDDYG--------KDLTS----VNI 1417
Cdd:pfam15921  666 rnELNSLSEDYEVLKRNFRNKSEEMeTTTNKLKMQLKSAqSELEQTRNTLKSMEGSDGHAmkvamgmqKQITAkrgqIDA 745
                          490       500       510
                   ....*....|....*....|....*....|..
gi 117938332  1418 LLKKQQMLENQMEVRKKEIEELQSQAQALSQE 1449
Cdd:pfam15921  746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
PH_SKIP cd13309
SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called ...
2199-2306 1.21e-03

SifA and kinesin-interacting protein Pleckstrin homology (PH) domain; SKIP (also called PLEKHM2/Pleckstrin homology domain-containing family M member 2) is a soluble cytosolic protein that contains a RUN domain and a PH domain separated by a unstructured linker region. SKIP is a target of the Salmonella effector protein SifA and the SifA-SKIP complex regulates kinesin-1 on the bacterial vacuole. The PH domain of SKIP binds to the N-terminal region of SifA while the N-terminus of SKIP is proposed to bind the TPR domain of the kinesin light chain. The opposite side of the SKIP PH domain is proposed to bind phosphoinositides. TSifA, SKIP, SseJ, and RhoA family GTPases are also thought to promote host membrane tubulation. Recently, it was shown that the lysosomal GTPase Arl8 binds to the kinesin-1 linker SKIP and that both are required for the normal intracellular distribution of lysosomes. Interestingly, two kinesin light chain binding motifs (WD) in SKIP have now been identified to match a consensus sequence for a kinesin light chain binding site found in several proteins including calsyntenin-1/alcadein, caytaxin, and vaccinia virus A36. SKIP has also been shown to interact with Rab1A. 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: 270119  Cd Length: 103  Bit Score: 40.44  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNRKheweAHNKKASSRSWHNVYCVINNQEMGFYKDAksaasgipyHSEVP---VSLKEAICEVA--LDYKKKKHV 2273
Cdd:cd13309     2 KEGMLMYK----TGTSYLGGETWKPGYFLLKNGVLYQYPDR---------SDRLPllsISLGGEQCGGCrrINNTERPHT 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 117938332 2274 FKLRLSDGNEYLFQAKDDEEMNTWIQAISSAIS 2306
Cdd:cd13309    69 FELILTDRSSLELAAPDEYEASEWLQSLCQSAS 101
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
2199-2307 1.45e-03

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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: 270070  Cd Length: 98  Bit Score: 39.90  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2199 MEGFLNrkheweahnKKASS--RSWHNVYCVINNQEMGFYKDAKSAASGIpyhseVPVSLKeaICEVALDYK-KKKHVFK 2275
Cdd:cd13250     1 KEGYLF---------KRSSNafKTWKRRWFSLQNGQLYYQKRDKKDEPTV-----MVEDLR--LCTVKPTEDsDRRFCFE 64
                          90       100       110
                  ....*....|....*....|....*....|..
gi 117938332 2276 LrLSDGNEYLFQAKDDEEMNTWIQAISSAISS 2307
Cdd:cd13250    65 V-ISPTKSYMLQAESEEDRQAWIQAIQSAIAS 95
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
40-158 1.50e-03

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 40.73  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   40 FERSRIKALAD---EREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLP------KPTKGRMRI 110
Cdd:cd21338     3 FERDAFDTLFDhapDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhnfylTPESFDQKV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 117938332  111 HcleNVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQ 158
Cdd:cd21338    83 H---NVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYK 127
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
2200-2306 1.98e-03

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. 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: 270118  Cd Length: 113  Bit Score: 40.08  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2200 EGFLNRKheweAHNKKASSRsWHNVYCVINNQEMGFYKDAKSAA-SGIPYHSEVPVSLKEAICevaldyKKKKHVFKL-- 2276
Cdd:cd13308    12 SGTLTKK----GGSQKTLQN-WQLRYVIIHQGCVYYYKNDQSAKpKGVFSLNGYNRRAAEERT------SKLKFVFKIih 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 117938332 2277 RLSDGNEYLFQAKDDEEMNTWIQAISSAIS 2306
Cdd:cd13308    81 LSPDHRTWYFAAKSEDEMSEWMEYIRREID 110
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
56-154 2.28e-03

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: 40.81  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNS---------HLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 123
Cdd:cd21325    25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 117938332  124 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 154
Cdd:cd21325   105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
56-154 2.66e-03

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: 40.38  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332   56 QKKTFTKWVNS---------HLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 123
Cdd:cd21324    25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 117938332  124 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 154
Cdd:cd21324   105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1528-1951 2.75e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1528 QTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAE------AIRQRLADlkqlwgllIEETEKRHRRLEEAhkaqqyyFDA 1601
Cdd:PRK02224  338 QAHNEEAESLREDADDLEERAEELREEAAELESEleeareAVEDRREE--------IEELEEEIEELRER-------FGD 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1602 AEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDyAETVHQLSK--TSRALVADShPESERISMRQSKVDKL 1679
Cdd:PRK02224  403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEALLEAGKcpECGQPVEGS-PHVETIEEDRERVEEL 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1680 YAGLKDLaEERRGKLDERH----RLFQLNREVDDLEQ--------------WIAE-REVVAGSHELGQDYEHVTMLQERF 1740
Cdd:PRK02224  481 EAELEDL-EEEVEEVEERLeraeDLVEAEDRIERLEErredleeliaerreTIEEkRERAEELRERAAELEAEAEEKREA 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1741 REFARDTGNIGQERVDTVNNMADEL------INSGHSDAATIAEWKDG---LNEAWADLLELIDTRTQILAASyelhkfy 1811
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELkeriesLERIRTLLAAIADAEDEierLREKREALAELNDERRERLAEK------- 632
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1812 hdakeifgriQDKHKKLPEELgrDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGdkaddiQKRENEVLE 1891
Cdd:PRK02224  633 ----------RERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA------VENELEELE 694
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1892 AWKSLLDACEGRRVRLVDtgdkfrffsmVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMN 1951
Cdd:PRK02224  695 ELRERREALENRVEALEA----------LYDEAEELESMYGDLRAELRQRNVETLERMLN 744
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
2214-2304 5.15e-03

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: 38.41  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2214 KKASS--RSWHNVYCVINNQEMGFYKDAK--SAASGIP---YHSEVPVSLKEAicevaldykKKKHVFKLRLSDGNEYLF 2286
Cdd:cd13248    15 KQGGSglKNWRKRWFVLKDNCLYYYKDPEeeKALGSILlpsYTISPAPPSDEI---------SRKFAFKAEHANMRTYYF 85
                          90
                  ....*....|....*...
gi 117938332 2287 QAKDDEEMNTWIQAISSA 2304
Cdd:cd13248    86 AADTAEEMEQWMNAMSLA 103
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1403-2071 5.70e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.05  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1403 IQSDDYGKDLTSVNIL-LKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLSERKHNL 1481
Cdd:COG0419   149 LKSKPKERKEILDELFgLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEE 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1482 LASKEIHQFNRDVEDEIlwvgermplatstdhghnlQTVQLLIKKNQTLQKEiqghqpriddifersQNIITDSSSLNAE 1561
Cdd:COG0419   229 ELEQEIEALEERLAELE-------------------EEKERLEELKARLLEI---------------ESLELEALKIREE 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1562 AIRQRLADLKQlWGLLIEETEKRHRRLEEAhKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAV 1641
Cdd:COG0419   275 ELRELERLLEE-LEEKIERLEELEREIEEL-EEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEK 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1642 EDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDE-RHRLFQLNREVDDLEQwiaerevv 1720
Cdd:COG0419   353 NELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEiQEELEELEKELEELER-------- 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1721 agshELGQDYEHVTMLQERFREFARDTGNIGQERvdtvnnmadelinsGHSDAATIAeWKDGLNEAWADLLELIDTRTQI 1800
Cdd:COG0419   425 ----ELEELEEEIKKLEEQINQLESKELMIAELA--------------GAGEKCPVC-GQELPEEHEKELLELYELELEE 485
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1801 LAASYELHKfyhDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKAD 1880
Cdd:COG0419   486 LEEELSREK---EEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELR 562
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1881 DIQKRENEVLEAWKSLLDACEGR------RVRLVDTGDKFRFfsmvrdlmlwmedvIRQIEAQEKpRDVSSVELLMNNHQ 1954
Cdd:COG0419   563 QLEDRLQELKELLEELRLLRTRKeeleelRERLKELKKKLKE--------------LEERLSQLE-ELLQSLELSEAENE 627
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 1955 GIKAEIDARNDSFTacIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLL 2034
Cdd:COG0419   628 LEEAEEELESELEK--LNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELE 705
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 117938332 2035 GQEPYLSS-----REIGQSVDEVEKLIKRHEAFEKSAATWDE 2071
Cdd:COG0419   706 ELLKKLGEieqliEELESRKAELEELKKELEKLEKALELLEE 747
PH_ASAP cd13251
ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs ...
2201-2305 6.99e-03

ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain; ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) 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: 270071  Cd Length: 108  Bit Score: 38.50  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2201 GFLNRKHEWEAHnkkassRSWHNVYCVINNQEMGFYkdakSAASGIPyhsevPVSLKEAICEVALDYKKKKHvFKLRLSD 2280
Cdd:cd13251    14 GYLLKKSEGKIR------KVWQKRRCSIKDGFLTIS----HADENKP-----PAKLNLLTCQVKLVPEDKKC-FDLISHN 77
                          90       100
                  ....*....|....*....|....*
gi 117938332 2281 GNeYLFQAKDDEEMNTWIQAISSAI 2305
Cdd:cd13251    78 RT-YHFQAEDENDANAWMSVLKNSK 101
PH_CNK_insect-like cd13326
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
2200-2301 7.65e-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: 37.71  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117938332 2200 EGFLNRKheweahNKKASSRS-WHNVYCVINNQEMGFYKDAKSA-ASGIPYHSEVPVSLKEaicEValdyKKKKHVFKLR 2277
Cdd:cd13326     2 QGWLYQR------RRKGKGGGkWAKRWFVLKGSNLYGFRSQESTkADCVIFLPGFTVSPAP---EV----KSRKYAFKVY 68
                          90       100
                  ....*....|....*....|....
gi 117938332 2278 LSdGNEYLFQAKDDEEMNTWIQAI 2301
Cdd:cd13326    69 HT-GTVFYFAAESQEDMKKWLDLL 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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