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Conserved domains on  [gi|2582814608|ref|NP_001411441|]
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plastin-2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 98-242 2.58e-104

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: 311.91  E-value: 2.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 242
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 374-507 4.57e-93

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).


The actual alignment was detected with superfamily member cd21331:

Pssm-ID: 469584  Cd Length: 134  Bit Score: 282.66  E-value: 4.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 374 YPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 453
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 454 MKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 251-375 6.53e-91

second 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 contaisn 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: 409176  Cd Length: 125  Bit Score: 276.84  E-value: 6.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 251 LLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDD 330
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 331 IQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 375
Cdd:cd21327    81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 511-625 3.94e-80

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


:

Pssm-ID: 409182  Cd Length: 115  Bit Score: 248.37  E-value: 3.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 511 GGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMA 590
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 591 RKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 13-79 2.25e-14

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


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 67.96  E-value: 2.25e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 98-242 2.58e-104

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: 311.91  E-value: 2.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 242
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 374-507 4.57e-93

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: 282.66  E-value: 4.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 374 YPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 453
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 454 MKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 251-375 6.53e-91

second 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 contaisn 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: 409176  Cd Length: 125  Bit Score: 276.84  E-value: 6.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 251 LLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDD 330
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 331 IQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 375
Cdd:cd21327    81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-620 2.96e-80

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 265.65  E-value: 2.96e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  16 EAFAKVDTDGNGYISCNELNDLFKAACL----PLPgYRVREITENLmatgdldqDGKISFDEFIkvfhGLKSTEVAKTFR 91
Cdd:COG5069    28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENV--------SGRLEFIKGK----GVKLFNIGPQDI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  92 KAINKKEGIcaiGGTSEQSSVGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFNAVGDGIVLCKMINLSV 171
Cdd:COG5069    95 VDGNPKLIL---GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 172 PDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIELSRNE 246
Cdd:COG5069   169 PDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIALHR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 247 aLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavvidmsGLR 326
Cdd:COG5069   245 -VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA----------PLE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 327 EKDDIQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPAL------HKPENQDIDwgaLEGEtREERTF 400
Cdd:COG5069   313 TTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVF 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 401 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVDLGKNQAkFSLVG 477
Cdd:COG5069   385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 478 IAGQDLNEGNRtLTLALVWQLMRRYTLNILEDIG-GGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLP-VLDL 555
Cdd:COG5069   464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582814608 556 IDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVNPKM-VMTVFACLM 620
Cdd:COG5069   543 LKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 511-625 3.94e-80

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


Pssm-ID: 409182  Cd Length: 115  Bit Score: 248.37  E-value: 3.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 511 GGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMA 590
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 591 RKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 120-235 1.44e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.73  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 120 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKkltPFTIQENLNLALN 199
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2582814608 200 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 235
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 124-234 1.08e-21

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: 90.07  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  124 YAFVNWINKALENDPdcrhvipmNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 203
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2582814608  204 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 234
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 264-376 1.51e-21

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 90.04  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 264 LSPEELLLRWANYHLENAG-CTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavviDMSGLREKDDIQRAECMLQQAE 342
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDK-------KKLNKSEFDKLENINLALDVAE 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 343 R-LGCRQF-VTATDVVRGNPKLNLAFIANLFNKYPA 376
Cdd:pfam00307  74 KkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 518-625 2.69e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.49  E-value: 2.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLKTENlddEEKLNNAKYAISMAR-KIGAR 596
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFTT-DLRDGLALCALLNKLAPGLVDKKKLNKSE---FDKLENINLALDVAEkKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2582814608 597 VYAL-PEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 396-502 1.17e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 81.56  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPypklggnMKKLENCNYAVDLGKN 469
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 470 QAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 268-373 2.32e-16

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: 74.66  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  268 ELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeeGIPAVVIDMSGLREKdDIQRAECMLQQAERLGC- 346
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPG----LVDKKKVAASLSRFK-KIENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 2582814608  347 RQFVTATDVVRGnPKLNLAFIANLFNK 373
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 398-501 8.45e-16

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: 73.12  E-value: 8.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  398 RTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVP-VDWNRVNKPPYPklggnMKKLENCNYAVDLGKNQaKF 473
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEKL-GG 74

                           90       100
                   ....*....|....*....|....*...
gi 2582814608  474 SLVGIAGQDLNEGNRtLTLALVWQLMRR 501
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 13-79 2.25e-14

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 67.96  E-value: 2.25e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 519-620 1.31e-13

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: 66.96  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  519 DIIVNWVNTTLKEAqKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARKIG-ARV 597
Cdd:smart00033   1 KTLLRWVNSLLAEY-DKPPVTNFSS-DLKDGVALCALLNSLSPGLVDKKKV-AASLSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 2582814608  598 YALPEDLVEVnPKMVMTVFACLM 620
Cdd:smart00033  78 LFEPEDLVEG-PKLILGVIWTLI 99
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-83 4.77e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 4.77e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFHGLKS 83
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRRLLTALGVS------EEEADELFARLDTDGDGKISFEEFVAAVRDYYT 134
EF-hand_7 pfam13499
EF-hand domain pair;
11-78 6.00e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 6.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582814608  11 MMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyRVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELY 66
PTZ00183 PTZ00183
centrin; Provisional
 2-77 1.94e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 48.15  E-value: 1.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2582814608   2 ARGSVSDEEMMELREAFAKVDTDGNGYISCNElndlFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00183    7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 13-40 6.20e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.36  E-value: 6.20e-04
                           10        20
                   ....*....|....*....|....*...
gi 2582814608   13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 98-242 2.58e-104

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: 311.91  E-value: 2.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 242
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 98-242 3.74e-98

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: 296.15  E-value: 3.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21324     1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 242
Cdd:cd21324    81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 98-245 7.00e-96

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: 290.42  E-value: 7.00e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21325     1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRN 245
Cdd:cd21325    81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 98-242 2.44e-94

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 286.55  E-value: 2.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  98 EGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21323     1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 178 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 242
Cdd:cd21323    81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 374-507 4.57e-93

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: 282.66  E-value: 4.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 374 YPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 453
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 454 MKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 251-375 6.53e-91

second 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 contaisn 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: 409176  Cd Length: 125  Bit Score: 276.84  E-value: 6.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 251 LLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDD 330
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 331 IQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 375
Cdd:cd21327    81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 383-507 3.77e-88

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: 269.55  E-value: 3.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 383 QDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNY 462
Cdd:cd21330     1 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 463 AVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21330    81 AVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 390-507 1.94e-80

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: 249.52  E-value: 1.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 390 LEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVDLGKN 469
Cdd:cd21329     1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2582814608 470 QAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21329    81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-620 2.96e-80

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 265.65  E-value: 2.96e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  16 EAFAKVDTDGNGYISCNELNDLFKAACL----PLPgYRVREITENLmatgdldqDGKISFDEFIkvfhGLKSTEVAKTFR 91
Cdd:COG5069    28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENV--------SGRLEFIKGK----GVKLFNIGPQDI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  92 KAINKKEGIcaiGGTSEQSSVGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFNAVGDGIVLCKMINLSV 171
Cdd:COG5069    95 VDGNPKLIL---GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 172 PDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIELSRNE 246
Cdd:COG5069   169 PDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIALHR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 247 aLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavvidmsGLR 326
Cdd:COG5069   245 -VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA----------PLE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 327 EKDDIQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPAL------HKPENQDIDwgaLEGEtREERTF 400
Cdd:COG5069   313 TTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVF 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 401 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVDLGKNQAkFSLVG 477
Cdd:COG5069   385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 478 IAGQDLNEGNRtLTLALVWQLMRRYTLNILEDIG-GGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLP-VLDL 555
Cdd:COG5069   464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582814608 556 IDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVNPKM-VMTVFACLM 620
Cdd:COG5069   543 LKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 511-625 3.94e-80

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


Pssm-ID: 409182  Cd Length: 115  Bit Score: 248.37  E-value: 3.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 511 GGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMA 590
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 591 RKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 390-507 6.05e-77

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: 240.22  E-value: 6.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 390 LEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVDLGKN 469
Cdd:cd21298     1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2582814608 470 QaKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21298    81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 251-372 5.70e-72

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


Pssm-ID: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 227.54  E-value: 5.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 251 LLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDD 330
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2582814608 331 IQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 372
Cdd:cd21328    81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 254-372 2.63e-67

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 214.83  E-value: 2.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 254 EGESLEDLMKLSPEELLLRWANYHLENAGCTK-ITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavviDMSGLREKDDIQ 332
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIKDSEAYTHLLKQIAPKDAGV-------DTSALRESDLLQ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2582814608 333 RAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 372
Cdd:cd21295    74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 516-627 3.00e-67

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


Pssm-ID: 409183  Cd Length: 112  Bit Score: 214.75  E-value: 3.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 516 VNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMARKIGA 595
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 596 RVYALPEDLVEVNPKMVMTVFACLMGKGMKRV 627
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 254-375 1.01e-65

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 210.90  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 254 EGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGiPAVVIDMSGLREKDDIQR 333
Cdd:cd21326     1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFD-ENIEIDFSGFNEKNDLKR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2582814608 334 AECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 375
Cdd:cd21326    80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 516-623 4.81e-63

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


Pssm-ID: 409150  Cd Length: 107  Bit Score: 203.28  E-value: 4.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 516 VNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENlDDEEKLNNAKYAISMARKIGA 595
Cdd:cd21301     1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGN-SEEDKLSNAKYAISMARKIGA 79

                          90       100
                  ....*....|....*....|....*...
gi 2582814608 596 RVYALPEDLVEVNPKMVMTVFACLMGKG 623
Cdd:cd21301    80 RVYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 509-623 9.89e-62

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


Pssm-ID: 409181  Cd Length: 115  Bit Score: 200.17  E-value: 9.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 509 DIGGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS 588
Cdd:cd21332     1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 589 MARKIGARVYALPEDLVEVNPKMVMTVFACLMGKG 623
Cdd:cd21332    81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 392-507 1.35e-54

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: 181.33  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 392 GETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKppyPKLGGNMKKLENCNYAVDLGKNQ 470
Cdd:cd21219     1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNK---PKPLNKFKKVENCNYAVDLAKKL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2582814608 471 aKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21219    78 -GFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 121-233 5.45e-53

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 177.00  E-value: 5.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 121 EEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKK-LTPFTIQENLNLALN 199
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 200 SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21217    81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 516-620 3.86e-48

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 163.59  E-value: 3.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 516 VNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARKIGA 595
Cdd:cd21220     1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLV-TEGETDEEKEQNAKYAISLARKIGA 79

                          90       100
                  ....*....|....*....|....*
gi 2582814608 596 RVYALPEDLVEVNPKMVMTVFACLM 620
Cdd:cd21220    80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 390-507 8.78e-45

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: 155.27  E-value: 8.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 390 LEGEtREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIkVP--VDWNRVNKPPYPKLGGNMKKLENCNYAVDLG 467
Cdd:cd21300     3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2582814608 468 KNQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21300    81 KQL-GFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 122-234 1.55e-44

first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409142  Cd Length: 116  Bit Score: 154.22  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTIN-KKKLTPFTIQENLNLALNS 200
Cdd:cd21293     2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKI 234
Cdd:cd21293    82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 116-235 5.65e-43

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: 150.29  E-value: 5.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 116 HSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINK-----KKLTPFTI 190
Cdd:cd21294     1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 191 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 235
Cdd:cd21294    81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 256-372 8.13e-42

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: 147.06  E-value: 8.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 256 ESLEDLMKLSPEELLLRWANYHLENAGCTK--ITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavVIDMSGLREKDDIQR 333
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDK-----ELVLEVLSEEDLEKR 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2582814608 334 AECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 372
Cdd:cd21218    76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 392-507 4.64e-34

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: 125.31  E-value: 4.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 392 GETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPyPKLggNMKKLENCNYAVDLGKnQ 470
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPgSVNWKHANKPP-IKM--PFKKVENCNQVVKIGK-Q 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2582814608 471 AKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNIL 507
Cdd:cd21299    77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 256-372 1.28e-33

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 124.21  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 256 ESLEDLMKLSPEELLLRWANYHLENAGCT-KITNFSTDIKDSKAYYHLLEQVAPKgdeegipavVIDMSGLREKDDIQRA 334
Cdd:cd21297     1 ETLEQFLRLPPEQILLRWFNYHLKAANWPrRVSNFSKDVSDGENYTVLLNQLAPE---------LCSRAPLQTTDLLQRA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2582814608 335 ECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 372
Cdd:cd21297    72 EQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 256-371 1.50e-32

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 121.09  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 256 ESLEDLMKLSPEELLLRWANYHLENAGCTK-ITNFSTDIKDSKAYYHLLEQVAPKGdeegipavvIDMSGLREKDDIQRA 334
Cdd:cd21296     1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSDVKDAEAYAYLLNVLAPEH---------CDPATLEAKDPLERA 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2582814608 335 ECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLF 371
Cdd:cd21296    72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 513-620 1.20e-31

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


Pssm-ID: 409152  Cd Length: 108  Bit Score: 118.68  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 513 GQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARK 592
Cdd:cd21303     1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLV-TPGNTEDEAYLNAKLAISIARK 79

                          90       100
                  ....*....|....*....|....*...
gi 2582814608 593 IGARVYALPEDLVEVNPKMVMTVFACLM 620
Cdd:cd21303    80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 516-620 1.27e-25

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


Pssm-ID: 409151  Cd Length: 109  Bit Score: 101.48  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 516 VNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARKIGA 595
Cdd:cd21302     2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLV-TKGETDEEKRLNATYIISVARKLGC 80

                          90       100
                  ....*....|....*....|....*
gi 2582814608 596 RVYALPEDLVEVNPKMVMTVFACLM 620
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 120-235 1.44e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.73  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 120 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKkltPFTIQENLNLALN 199
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2582814608 200 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 235
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 124-234 1.08e-21

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: 90.07  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  124 YAFVNWINKALENDPdcrhvipmNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 203
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2582814608  204 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 234
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 264-376 1.51e-21

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 90.04  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 264 LSPEELLLRWANYHLENAG-CTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavviDMSGLREKDDIQRAECMLQQAE 342
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDK-------KKLNKSEFDKLENINLALDVAE 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 343 R-LGCRQF-VTATDVVRGNPKLNLAFIANLFNKYPA 376
Cdd:pfam00307  74 KkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 518-625 2.69e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.49  E-value: 2.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLKTENlddEEKLNNAKYAISMAR-KIGAR 596
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFTT-DLRDGLALCALLNKLAPGLVDKKKLNKSE---FDKLENINLALDVAEkKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2582814608 597 VYAL-PEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 396-502 1.17e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 81.56  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPypklggnMKKLENCNYAVDLGKN 469
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 470 QAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 268-373 2.32e-16

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: 74.66  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  268 ELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeeGIPAVVIDMSGLREKdDIQRAECMLQQAERLGC- 346
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPG----LVDKKKVAASLSRFK-KIENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 2582814608  347 RQFVTATDVVRGnPKLNLAFIANLFNK 373
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 123-233 2.68e-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 [Multi-domain]  Cd Length: 103  Bit Score: 74.68  E-value: 2.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 123 KYAFVNWINKALENDPdcrhvipmNPNTDDLFNAVGDGIVLCKMINLSVPDTIDErtINKKKLTPFTIQENLNLALNSAS 202
Cdd:cd00014     1 EEELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACK 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 203 AIG-CHVVNIGAEDLKEGK-PYLVLGLLWQVIK 233
Cdd:cd00014    71 KLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 398-501 8.45e-16

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: 73.12  E-value: 8.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  398 RTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVP-VDWNRVNKPPYPklggnMKKLENCNYAVDLGKNQaKF 473
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEKL-GG 74

                           90       100
                   ....*....|....*....|....*...
gi 2582814608  474 SLVGIAGQDLNEGNRtLTLALVWQLMRR 501
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 13-79 2.25e-14

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 67.96  E-value: 2.25e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 519-620 1.31e-13

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: 66.96  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  519 DIIVNWVNTTLKEAqKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARKIG-ARV 597
Cdd:smart00033   1 KTLLRWVNSLLAEY-DKPPVTNFSS-DLKDGVALCALLNSLSPGLVDKKKV-AASLSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 2582814608  598 YALPEDLVEVnPKMVMTVFACLM 620
Cdd:smart00033  78 LFEPEDLVEG-PKLILGVIWTLI 99
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 119-233 1.78e-13

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 66.92  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 119 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKK-LTPFTIQENLNLA 197
Cdd:cd21219     3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKpLNKFKKVENCNYA 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 198 LNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21219    71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 120-232 1.95e-11

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: 61.15  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 120 EEEKYAFVNWINKALEndpdcrhviPMNPNTDDLFNAVGDGIVLCKMInlsvpDTIDERTI---NKKKLTPFTIQENLNL 196
Cdd:cd21227     3 EIQKNTFTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALV-----EILQGRKLgrvIKKPLNQHQKLENVTL 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 197 ALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21227    69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 396-502 3.99e-11

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: 60.11  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS-LGVNPR-VNHLYSDLSDALVIFQLYEKIkvpvdwNRVNKPPY---PKLggNMKKLENCNYAVDLGKNQ 470
Cdd:cd21215     5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIKSR 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 471 aKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21215    77 -GVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-83 4.77e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 4.77e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFHGLKS 83
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRRLLTALGVS------EEEADELFARLDTDGDGKISFEEFVAAVRDYYT 134
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 122-232 5.82e-10

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: 57.15  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALEndpdcRHVIPMNPNtdDLFNAVGDGIVLCKMIN-LSVPDTIDERTINkkkltPFTIQENLNLALNS 200
Cdd:cd21242     6 QKRTFTNWINSQLA-----KHSPPSVVS--DLFTDIQDGHRLLDLLEvLSGQQLPREKGHN-----VFQCRSNIETALSF 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21242    74 LKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
EF-hand_7 pfam13499
EF-hand domain pair;
11-78 6.00e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 6.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582814608  11 MMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyRVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 389-501 6.37e-10

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: 57.73  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 389 ALEGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDL 466
Cdd:cd21318    32 ADEREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLS----GEQLPKPTRGRM--RIHSLENVDKALQF 105

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 467 GKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21318   106 LKEQ-RVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 389-501 7.02e-10

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: 56.99  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 389 ALEGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDL 466
Cdd:cd21246    10 ADEREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGKM--RIHCLENVDKALQF 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 467 GKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21246    84 LKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 396-501 7.48e-10

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: 56.92  E-value: 7.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDLGKNQAKF 473
Cdd:cd21193    17 QKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIIS----GEKLGKPNRGRL--RVQKIENVNKALAFLKTKVRL 90

                          90       100
                  ....*....|....*....|....*...
gi 2582814608 474 SLVGiaGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21193    91 ENIG--AEDIVDGNPRLILGLIWTIILR 116
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 119-233 1.14e-09

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: 56.09  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 119 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINK---KKLTPFTIQENLN 195
Cdd:cd21298     5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2582814608 196 LALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21298    73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 122-232 2.37e-09

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: 55.38  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALEndpDCRHVIpmnpntDDLFNAVGDGIVLCKMINLSVPDTIDErtINKKKLTPFTIqENLNLALNSA 201
Cdd:cd21193    17 QKKTFTKWINSFLE---KANLEI------GDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAiGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21193    85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 122-241 2.42e-09

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: 55.07  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALendpdCRHVIPMNpnTDDLFNAVGDGIVLCKMIN-LSVPDTIDERTINKKKLTPFTiqeNLNLALNS 200
Cdd:cd21241     6 QKKTFTNWINSYL-----AKRKPPMK--VEDLFEDIKDGTKLLALLEvLSGEKLPCEKGRRLKRVHFLS---NINTALKF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIkigLFADIE 241
Cdd:cd21241    76 LESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 120-236 3.00e-09

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: 55.12  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 120 EEEKYAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKK----LTPFTIQENLN 195
Cdd:cd21300     6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2582814608 196 LALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGL 236
Cdd:cd21300    75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHI 115
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 391-505 6.18e-09

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: 54.61  E-value: 6.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVD- 465
Cdd:cd21236    13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL---------SGDTLPREKGRMRfhRLQNVQIALDy 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2582814608 466 LGKNQAKfsLVGIAGQDLNEGNRTLTLALVWQLMRRYTLN 505
Cdd:cd21236    84 LKRRQVK--LVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 391-501 1.04e-08

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: 53.90  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS-LG-VNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDLGK 468
Cdd:cd21317    27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLS----GEQLPKPTKGRM--RIHCLENVDKALQFLK 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 469 NQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21317   101 EQ-KVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4-93 2.83e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608   4 GSVSDEEMMELREA-----FAKVDTDGNGYISCNElndlFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:COG5126    20 GVLERDDFEALFRRlwatlFSEADTDGDGRISREE----FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL 95

                          90
                  ....*....|....*..
gi 2582814608  79 --HGLKSTEVAKTFRKA 93
Cdd:COG5126    96 taLGVSEEEADELFARL 112
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 122-232 3.24e-08

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: 51.63  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMI-NLSvpdtiDERTINKKKLTPFTIQENLNLALNS 200
Cdd:cd21188     4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLeVLS-----GESLPRERGRMRFHRLQNVQTALDF 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21188    70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 122-233 4.30e-08

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: 51.63  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALEndpdcRHVIPMNPNTDDLfnavGDGIVLCKMInlsvpDTIDERTINKKKLTP-FTIQ--ENLNLAL 198
Cdd:cd21215     5 QKKTFTKWLNTKLS-----SRGLSITDLVTDL----SDGVRLIQLL-----EIIGDESLGRYNKNPkMRVQklENVNKAL 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 199 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21215    71 EFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 122-241 8.54e-08

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: 51.03  E-value: 8.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALEndpdcRHVIPMNpnTDDLFNAVGDGIVLCKMINLSVPDTIDERTinKKKLTPFTIQENLNLALNSA 201
Cdd:cd21190     6 QKKTFTNWINSHLA-----KLSQPIV--INDLFVDIKDGTALLRLLEVLSGQKLPIES--GRVLQRAHKLSNIRNALDFL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIkigLFADIE 241
Cdd:cd21190    77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 396-496 1.15e-07

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: 50.09  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVDLGKNQa 471
Cdd:cd21188     4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL---------SGESLPRERGRMRfhRLQNVQTALDFLKYR- 73

                          90       100
                  ....*....|....*....|....*
gi 2582814608 472 KFSLVGIAGQDLNEGNRTLTLALVW 496
Cdd:cd21188    74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 518-613 1.28e-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: 50.38  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQKSSS-IASFkDPKISTSLPVLDLIDAIQPGSINyDLLKTENLDDEEKLNNAKYAISMARKIGAR 596
Cdd:cd21218    12 EEILLRWVNYHLKKAGPTKKrVTNF-SSDLKDGEVYALLLHSLAPELCD-KELVLEVLSEEDLEKRAEKVLQAAEKLGCK 89

                          90
                  ....*....|....*..
gi 2582814608 597 VYALPEDLVEVNPKMVM 613
Cdd:cd21218    90 YFLTPEDIVSGNPRLNL 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 375-506 2.79e-07

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: 49.64  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 375 PALHKPENQDIDWGALEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLGG 452
Cdd:cd21310     1 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLS----QKKMYRKYHPRPNF 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 453 NMKKLENCNYAVDLgKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNI 506
Cdd:cd21310    72 RQMKLENVSVALEF-LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 410-500 3.25e-07

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 49.11  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 410 NPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPyPKlgGNMKKLENCNYAVDlGKNQAKFSLVGIAGQDLNEGN 487
Cdd:cd21217    27 DPDGDDLFEALRDGVLLCKLINKIV-PgtIDERKLNKKK-PK--NIFEATENLNLALN-AAKKIGCKVVNIGPQDILDGN 101

                          90
                  ....*....|...
gi 2582814608 488 RTLTLALVWQLMR 500
Cdd:cd21217   102 PHLVLGLLWQIIR 114
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
14-96 3.33e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  14 LREAFAKVDTDGNGYISCNELNDLFKAAClplpgyrvreitENLMATGDLDQDGKISFDEFIKVFHGLKSTEVAKTFRKA 93
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDFEALFRRLW------------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAA 74


                  ...
gi 2582814608  94 INK 96
Cdd:COG5126    75 FDL 77
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 391-505 3.35e-07

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: 49.26  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYE---KIKVPVDWNRVNkppypklggnMKKLENCNYAVD 465
Cdd:cd21237     2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEvlsGVKLPREKGRMR----------FHRLQNVQIALD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2582814608 466 LGKnQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLN 505
Cdd:cd21237    72 FLK-QRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 396-502 4.26e-07

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: 48.82  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPklggnMKKLENCNYAVDLGKNQAkF 473
Cdd:cd21227     5 QKNTFTNWVNEQlkPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQ-----HQKLENVTLALKAMAEDG-I 78

                          90       100
                  ....*....|....*....|....*....
gi 2582814608 474 SLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21227    79 KLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 389-501 6.41e-07

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: 49.27  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 389 ALEGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDL 466
Cdd:cd21316    47 ADEREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQF 120

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2582814608 467 GKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21316   121 LKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 375-506 7.53e-07

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: 48.54  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 375 PALHKPENQDIDWGALEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKlgg 452
Cdd:cd21308     5 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR--- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 453 nMKKLENCNYAVDLgKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNI 506
Cdd:cd21308    77 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 375-506 8.69e-07

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: 48.54  E-value: 8.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 375 PALHKPENQDIDWGALEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKlgg 452
Cdd:cd21309     2 PVTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFR--- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582814608 453 nMKKLENCNYAVDLgKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNI 506
Cdd:cd21309    74 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 396-502 9.81e-07

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: 47.48  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPVDWNRvnKPPYPKlggnmKKLENCNYAVDLgKNQ 470
Cdd:cd21183     5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLstrPLKRSYNR--RPAFQQ-----HYLENVSTALKF-IEA 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 471 AKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21183    77 DHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 122-232 1.03e-06

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: 48.06  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDErtinKKKLTPFTIQENLNLALNSA 201
Cdd:cd21236    18 QKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21236    85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 16-77 1.73e-06

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 49.66  E-value: 1.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608  16 EAFAKVDTDGNGYISCNELNDLFKAACLPLPG-----YRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:cd15902     3 EVWMHFDADGNGYIEGKELDSFLRELLKALNGkdktdDEVAEKKKEFMEKYDENEDGKIEIRELANI 69
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 122-232 1.75e-06

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: 47.71  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENDPdCRhvipmnpnTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFtiqENLNLALNSA 201
Cdd:cd21318    39 QKKTFTKWVNSHLARVP-CR--------INDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21318   107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
PTZ00183 PTZ00183
centrin; Provisional
 2-77 1.94e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 48.15  E-value: 1.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2582814608   2 ARGSVSDEEMMELREAFAKVDTDGNGYISCNElndlFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00183    7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 13-74 1.95e-06

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 47.98  E-value: 1.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLpGYRVreiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16185     1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLF-SLAT---AEKLIRMFDRDGNGTIDFEEF 58
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 13-83 1.98e-06

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 48.29  E-value: 1.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAAClplpGYRVREITENLMATG-DLDQDGKISFDEFIKVFHGLKS 83
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGD----WTPFSIETVRLMINMfDRDRSGTINFDEFVGLWKYIQD 68
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 122-243 1.99e-06

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: 46.94  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDErtinKKKLTPFTIQENLNLALNSA 201
Cdd:cd21235     7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELS 243
Cdd:cd21235    74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 393-502 1.99e-06

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: 46.76  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 393 ETREERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKvpvdwNRVNKPPYPKLGGN-MKKLENCNYAVDLGK 468
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKrgiPKISDLATDLSDGVRLIFFLELVS-----GKKFPKKFDLEPKNrIQMIQNLHLAMLFIE 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 469 NQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21225    77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 122-232 2.40e-06

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: 46.71  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALEndpdCRhvipmNPNTDDLFNAVGDGIVLCKMINLsVPDTIDERTINKKKLTPFTIQENLNLALNSA 201
Cdd:cd21183     5 QANTFTRWCNEHLK----ER-----GMQIHDLATDFSDGLCLIALLEN-LSTRPLKRSYNRRPAFQQHYLENVSTALKFI 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21183    75 EADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 391-511 2.58e-06

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: 46.94  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVDL 466
Cdd:cd21235     2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 467 GKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNILEDIG 511
Cdd:cd21235    73 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSG 116
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 119-233 3.40e-06

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 46.52  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 119 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLS-VPdtIDERTINKKkltPFTIQ------ 191
Cdd:cd21329     5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTrVP--VDWGHVNKP---PYPALggnmkk 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2582814608 192 -ENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21329    68 iENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 13-74 4.00e-06

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 45.60  E-value: 4.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16251    35 QIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRDLTDEE-TKALLAAGDTDGDGKIGVEEF 95
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 393-499 4.85e-06

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: 45.46  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 393 ETREERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVDLGKNQ 470
Cdd:cd21214     3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVIS----GERLPKPERGKM--RFHKIANVNKALDFIASK 76

                          90       100
                  ....*....|....*....|....*....
gi 2582814608 471 AkFSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21214    77 G-VKLVSIGAEEIVDGNLKMTLGMIWTII 104
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 13-79 4.88e-06

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 45.58  E-value: 4.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREiTENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd16254    35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSDKE-TKALLAAGDKDGDGKIGIDEFATLVA 100
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 396-506 5.03e-06

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: 45.91  E-value: 5.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnRVNKPPypklggNMK--KLENCNYAVDLGK 468
Cdd:cd21311    16 QQNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsqKLENVSVALKFLE 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2582814608 469 NQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNI 506
Cdd:cd21311    86 EDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISM 123
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 396-502 5.20e-06

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: 45.56  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwNRVNKPPYPKLGGNMKKLENCNYAVDLGKNQaKF 473
Cdd:cd21228     5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQ----KRMYKKYNKRPTFRQMKLENVSVALEFLERE-SI 79

                          90       100
                  ....*....|....*....|....*....
gi 2582814608 474 SLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21228    80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 394-502 5.24e-06

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: 45.90  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 394 TREERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnrvnKPPYPKLggNMKKLENCNYAVDL 466
Cdd:cd21247    19 TMQKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELIsgeQLP-------RPSRGKM--RVHFLENNSKAITF 89

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 467 GKNQAKFSLVGiaGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21247    90 LKTKVPVKLIG--PENIVDGDRTLILGLIWIIILRF 123
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 396-496 6.91e-06

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: 45.07  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVD-LGKN 469
Cdd:cd21186     3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVL---------TGKKLKPEKGRMRvhHLNNVNRALQvLEQN 73

                          90       100
                  ....*....|....*....|....*..
gi 2582814608 470 QAKfsLVGIAGQDLNEGNRTLTLALVW 496
Cdd:cd21186    74 NVK--LVNISSNDIVDGNPKLTLGLVW 98
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 119-233 6.94e-06

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: 45.57  E-value: 6.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 119 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLT-PFTIQENLNLA 197
Cdd:cd21299     3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 198 LNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21299    71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
PTZ00184 PTZ00184
calmodulin; Provisional
 1-77 7.70e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.29  E-value: 7.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608   1 MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVreitENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00184   73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV----DEMIREADVDGDGQINYEEFVKM 145
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 396-499 8.24e-06

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: 45.00  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMN---SLGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVDLgKNQ 470
Cdd:cd21232     3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGL---------TGKSLPKERGSTRvhALNNVNRVLQV-LHQ 72

                          90       100
                  ....*....|....*....|....*....
gi 2582814608 471 AKFSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21232    73 NNVELVNIGGTDIVDGNHKLTLGLLWSII 101
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 13-74 8.64e-06

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 44.86  E-value: 8.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAAClplPGYRV---REiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16253    35 DIKKVFNILDQDKSGFIEEEELKLFLKNFS---DGARVlsdKE-TKNFLAAGDSDGDGKIGVDEF 95
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 267-374 1.44e-05

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: 44.44  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 267 EELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPavvidmsgLREKDDIQRAE----CMLQQAE 342
Cdd:cd21225     6 IKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFD--------LEPKNRIQMIQnlhlAMLFIEE 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 343 RLGCR-QFVTATDVVRGNPKLNLAFIANLFNKY 374
Cdd:cd21225    78 DLKIRvQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 122-232 1.54e-05

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: 44.67  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMIN-LSvpdtiDER--TINKKKLTPFTIqENLNLAL 198
Cdd:cd21246    17 QKKTFTKWVNS---------HLARVGCRINDLYTDLRDGRMLIKLLEvLS-----GERlpKPTKGKMRIHCL-ENVDKAL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 199 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21246    82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 122-233 1.98e-05

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 44.61  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMIN-LSVPdtIDERTINK----------KKLtpfti 190
Cdd:cd21331    23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKppypklganmKKL----- 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2582814608 191 qENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21331    85 -ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 7-98 2.62e-05

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 46.42  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608   7 SDEEMME-LREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyRVREITENLMATGDLDQDGKISFDEFIKVFHG----- 80
Cdd:cd16226    29 TPEESKErLGIIVDKIDKNGDGFVTEEELKDWIKYVQKK----YIREDVDRQWKEYDPNKDGKLSWEEYKKATYGfldde 104

                          90
                  ....*....|....*...
gi 2582814608  81 LKSTEVAKTFRKAINKKE 98
Cdd:cd16226   105 EEDDDLHESYKKMIRRDE 122
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 407-501 2.84e-05

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: 43.98  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 407 LGVNPRVNHLYSDLSDALVIFQLYEKIkVP--VDWNRVNKPPYP-KLGGNMKKLENCNYAVdlgkNQAK---FSLVGIAG 480
Cdd:cd21294    29 LPFPTDTFQLFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKnKPLNNFQMIENNNIVI----NSAKaigCSVVNIGA 103

                          90       100
                  ....*....|....*....|.
gi 2582814608 481 QDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21294   104 GDIIEGREHLILGLIWQIIRR 124
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 13-79 4.06e-05

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 42.80  E-value: 4.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNdLFkaacLPLPGYRVREITEN----LMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd16255    35 DVKKVFEIIDQDKSGFIEEEELK-LF----LQNFSSGARELTDAetkaFLKAGDSDGDGKIGVEEFQALVK 100
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 265-360 4.10e-05

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: 42.99  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 265 SPEELLLRWANYHLENAgctKITNFSTDIKDSKAYYHLLEQVAPkgdeEGIPavviDMSGLREKDDIQRAECMLQQAER- 343
Cdd:cd21184     1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKP----GLIP----DNESLDKENPLENATKAMDIAEEe 69

                          90
                  ....*....|....*..
gi 2582814608 344 LGCRQFVTATDVVRGNP 360
Cdd:cd21184    70 LGIPKIITPEDMVSPNV 86
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 7-76 4.23e-05

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 45.42  E-value: 4.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2582814608   7 SDEEMMElreAFAKVDTDGNGYISCNEL----NDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIK 76
Cdd:cd15902    88 SSVEFMK---IWRKYDTDGSGFIEAKELkgflKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 265-375 4.72e-05

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: 42.76  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 265 SPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeegipavVIDMSGLREKDDIQRAECMLQQAER- 343
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPD---------LIDFRSVRNQSNRENLENAFNVAEKe 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 344 LGCRQFVTATDVVRGNP--KLNLAFIANLFNKYP 375
Cdd:cd21189    72 FGVTRLLDPEDVDVPEPdeKSIITYVSSLYDVFP 105
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 518-619 6.01e-05

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 42.95  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQkSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLKTENL---DDEEKLNNAKYAISMARKIG 594
Cdd:cd21326    14 EELLLRWVNYHLTNAG-WQNISNFSQ-DIKDSRAYFHLLNQIAPKGDVFDENIEIDFsgfNEKNDLKRAEYMLQEADKLG 91

                          90       100
                  ....*....|....*....|....*
gi 2582814608 595 ARVYALPEDLVEVNPKMVMTVFACL 619
Cdd:cd21326    92 CRQFVTPADVVSGNPKLNLAFVANL 116
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 13-100 6.32e-05

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 43.75  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAAclplpGYRV-REITENLM---AtgdlDQDGKISFDEFIKVFHGLKSteVAK 88
Cdd:cd16182    73 KWQAIFKKFDTDRSGTLSSYELRKALESA-----GFHLsNKVLQALVlryA----DSTGRITFEDFVSCLVRLKT--AFE 141

                          90
                  ....*....|..
gi 2582814608  89 TFRKAINKKEGI 100
Cdd:cd16182   142 TFSALDKKNEGV 153
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 391-499 7.20e-05

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: 42.60  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVpvdwnrvNKPPYPKLGGNMKKLENCNYAVD-L 466
Cdd:cd21231     2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-------QKLVKEKGSTRVHALNNVNKALQvL 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 467 GKNQAkfSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21231    75 QKNNV--DLVNIGSADIVDGNHKLTLGLIWSII 105
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 15-77 7.73e-05

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 43.67  E-value: 7.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2582814608  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRV-REITENLMATGDLDQDGKISFDEFIKV 77
Cdd:cd16180    70 RRLFRRFDRDRSGSIDFNELQNALSSF-----GYRLsPQFVQLLVRKFDRRRRGSISFDDFVEA 128
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 256-380 7.79e-05

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: 42.37  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 256 ESLEDLMKLSPEELLLRWANYHLENagcTKITNFSTDIKDSKAYYHLLEQVApkgdeegiPAVVIDMSGLREKDDIQRAE 335
Cdd:cd21314     2 EDEEDARKQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCA--------PGLCPDWESWDPNQPVQNAR 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2582814608 336 CMLQQAER-LGCRQFVTATDVVrgNPKLNLAFIANLFNKYP-ALHKP 380
Cdd:cd21314    71 EAMQQADDwLGVPQVIAPEEIV--DPNVDEHSVMTYLSQFPkAKLKP 115
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 391-499 8.21e-05

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: 42.17  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS----LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKppypklggNMKKLENCNYA 463
Cdd:cd21190     1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2582814608 464 VDLGKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21190    73 LDFLTKR-CIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 122-228 8.87e-05

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: 41.80  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENDPDCRHVIpmnpntdDLFNAVGDGIVLCKMINLSVPDTIDErtINKKKLTPFTIQENLNLALNSA 201
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIIT-------DLQKDLGDGLTLVNLIEAVAGEKVPG--IHSRPKTRAQKLENIQACLQFL 71

                          90       100
                  ....*....|....*....|....*..
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLL 228
Cdd:cd21212    72 AALGVDVQGITAEDIVDGNLKAILGLF 98
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 121-232 9.07e-05

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: 41.99  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 121 EEKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERtiNKKKLTPFTIQeNLNLALNS 200
Cdd:cd21214     5 QQRKTFTAWCNS---------HLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIA-NVNKALDF 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21214    73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 122-232 9.55e-05

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: 42.18  E-value: 9.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENdpdCrhvipmNP--NTDDLFNAVGDGIVLCKMIN-LSVPDTIDERTINKKKLtpFTIQeNLNLAL 198
Cdd:cd21191     6 QKRTFTRWINLHLEK---C------NPplEVKDLFVDIQDGKILMALLEvLSGQNLLQEYKPSSHRI--FRLN-NIAKAL 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 199 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21191    74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 122-243 1.02e-04

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: 42.33  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMinLSVPDTIdeRTINKKKLTPFTIQENLNLALNSA 201
Cdd:cd21237     7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISL--LEVLSGV--KLPREKGRMRFHRLQNVQIALDFL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELS 243
Cdd:cd21237    74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 122-232 1.03e-04

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: 41.83  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENdpdCRhvipmNPNTDDLFNAVGDGIVLCKMINlsvpDTIDERTINKKKLTPFTIQENLNLALNSA 201
Cdd:cd21231     7 QKKTFTKWINAQFAK---FG-----KPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21231    75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 13-84 1.06e-04

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t specific neurons of the central and peripheral nervous system. It possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 44.10  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  13 ELREAFAKVDTDGNGYISCNE----LNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDE----------FIKVF 78
Cdd:cd16177    91 EFMEAWRKYDTDRSGYIEANElkgfLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEmarllpvqenFLLKF 170


                  ....*.
gi 2582814608  79 HGLKST 84
Cdd:cd16177   171 QGMKLS 176
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 391-499 1.13e-04

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: 41.74  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS-LGVNPR---VNHLYSDLSDALVIFQLYEKIKvpvdwnrVNKPPYPKLGGNMKKLENCNYAVDL 466
Cdd:cd21242     1 EQEQTQKRTFTNWINSqLAKHSPpsvVSDLFTDIQDGHRLLDLLEVLS-------GQQLPREKGHNVFQCRSNIETALSF 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 467 GKNQAkFSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21242    74 LKNKS-IKLINIHVPDIIEGKPSIILGLIWTII 105
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 267-371 1.22e-04

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 41.49  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 267 EELLLRWANYHLENAG-CTKITNFStD--IKDSKAYYHLLEQVAPKgdeegipaVVID---MSGLREKDDIQRAECMLQQ 340
Cdd:cd21220     3 DADILAWANSKVREAGkSSPISSFK-DpsLSTGLFLLDLLAAIDPG--------AVDYdlvTEGETDEEKEQNAKYAISL 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 341 AERLGCRQFVTATDVVRGNPKLNLAFIANLF 371
Cdd:cd21220    74 ARKIGAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 254-375 1.28e-04

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: 42.08  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 254 EGESLEDLMKLSPEELLLRWANYHLENagcTKITNFSTDIKDSKAYYHLLEQVApkgdeegiPAVVIDMSGLREKDDIQR 333
Cdd:cd21315     5 EDDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALA--------PGLCPDWEDWDPKDAVKN 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2582814608 334 AECMLQQAER-LGCRQFVTATDVVrgNPKLNLAFIANLFNKYP 375
Cdd:cd21315    74 AKEAMDLAEDwLDVPQLIKPEEMV--NPKVDELSMMTYLSQFP 114
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 122-232 1.31e-04

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: 42.35  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALENdPDCRhvipmnpnTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFtiqENLNLALNSA 201
Cdd:cd21317    32 QKKTFTKWVNSHLAR-VTCR--------IGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21317   100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 4-75 1.57e-04

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 42.57  E-value: 1.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2582814608   4 GSVSDEEMMEL-------REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFI 75
Cdd:cd16196    56 GKLGFEEFKKLwedlrswKRVFKLFDTDGSGSFSSFELRNALNSA-----GFRLSNATLNALVLRYSNKDGRISFDDFI 129
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 122-233 1.71e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 41.90  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFNAVGDGIVLCKMI-NLSVPdtIDERTINK----------KKLtpfti 190
Cdd:cd21330    14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2582814608 191 qENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 233
Cdd:cd21330    76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 13-40 1.72e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 38.92  E-value: 1.72e-04
                          10        20
                  ....*....|....*....|....*...
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 1-74 2.02e-04

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 40.98  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608   1 MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVR-EITENLMATGDLDQDGKISFDEF 74
Cdd:cd16252    26 MQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVAPLSdEEAEAMIQAADTDGDGRIDFQEF 100
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 267-372 2.26e-04

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 40.78  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 267 EELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeeGIPAVVID-MSGLREKDDIQRAecmLQQAERLG 345
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPG----SIPKINKKpKSPFKKRENINLF---LNACKKLG 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 2582814608 346 C--RQFVTATDVV-RGNPKLNLAFIANLFN 372
Cdd:cd00014    74 LpeLDLFEPEDLYeKGNLKKVLGTLWALAL 103
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 391-499 2.40e-04

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: 41.03  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNSL--GVNP--RVNHLYSDLSDALVIFQLYEKIKvpvDWNRVNKppYPKLGGNMKKLENCNYAVDL 466
Cdd:cd21191     1 ERENVQKRTFTRWINLHleKCNPplEVKDLFVDIQDGKILMALLEVLS---GQNLLQE--YKPSSHRIFRLNNIAKALKF 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 467 GKNQaKFSLVGIAGQDLNEGNRTLTLALVWQLM 499
Cdd:cd21191    76 LEDS-NVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 264-375 2.46e-04

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: 40.80  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 264 LSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeegipavVIDMSGLREKDDIQRAECMLQQAER 343
Cdd:cd21240     3 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPD---------LVDMERVQIQSNRENLEQAFEVAER 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2582814608 344 LGCRQFVTATDVVRGNP--KLNLAFIANLFNKYP 375
Cdd:cd21240    74 LGVTRLLDAEDVDVPSPdeKSVITYVSSIYDAFP 107
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 13-90 2.68e-04

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 42.03  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  13 ELREAFAKVDTDgNGYISCNELNDLFKAACLPLPGYRVR-EITENLMATGDLDQDGKISFDEFIKVFHGLKS-TEVAKTF 90
Cdd:cd15897     1 QLRNVFQAVAGD-DGEISATELQQALSNVGWTHFDLGFSlETCRSMIAMMDRDHSGKLNFSEFKGLWNYIKAwQEIFRTY 79
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 122-232 3.37e-04

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: 40.44  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKALeNDPDCRHVipmnpntDDLFNAVGDGIVLckminLSVPDTIDERTINKKK-LTPFTIQENLNLALNS 200
Cdd:cd21186     3 QKKTFTKWINSQL-SKANKPPI-------KDLFEDLRDGTRL-----LALLEVLTGKKLKPEKgRMRVHHLNNVNRALQV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21186    70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 16-79 3.39e-04

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 39.13  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2582814608  16 EAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00052     3 QIFRSLDPDGDGLISGDEARPFLGKSGLP------RSVLAQIWDLADTDKDGKLDKEEFAIAMH 60
EF-hand_6 pfam13405
EF-hand domain;
13-40 3.50e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.93  E-value: 3.50e-04
                          10        20
                  ....*....|....*....|....*...
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRS 28
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 273-370 3.60e-04

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: 40.26  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 273 WANYHLENAGCTK-ITNFSTDIKDSKAYYHLLEQVApkgdEEGIPAVvidmsGLREKDDIQRAE----CmLQQAERLGCR 347
Cdd:cd21212     8 WANHYLEKGGHKRiITDLQKDLGDGLTLVNLIEAVA----GEKVPGI-----HSRPKTRAQKLEniqaC-LQFLAALGVD 77

                          90       100
                  ....*....|....*....|....
gi 2582814608 348 -QFVTATDVVRGNPKLNLAFIANL 370
Cdd:cd21212    78 vQGITAEDIVDGNLKAILGLFFSL 101
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 555-614 3.69e-04

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 40.30  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2582814608 555 LIDAIQPGSINYdllkTENLDDEEKLNNAKYAISMA-RKIGARVYALPEDLV--EVNPKMVMT 614
Cdd:cd21184    35 LVDALKPGLIPD----NESLDKENPLENATKAMDIAeEELGIPKIITPEDMVspNVDELSVMT 93
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 14-100 3.86e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 41.11  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  14 LREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFHGLKST-EVAKTFRK 92
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVS----EKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERpELEPIFKK 77


                  ....*....
gi 2582814608  93 -AINKKEGI 100
Cdd:cd15898    78 yAGTNRDYM 86
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 125-229 4.50e-04

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: 40.21  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 125 AFVNWINKALENdpdcRHVIPMNPNTDDLfnavGDGIVLCKMINLsvpdtIDERTINKK-KLTPFT-IQ--ENLNLALNS 200
Cdd:cd21225     8 AFTAWVNSVLEK----RGIPKISDLATDL----SDGVRLIFFLEL-----VSGKKFPKKfDLEPKNrIQmiQNLHLAMLF 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 2582814608 201 ASA-IGCHVVNIGAEDLKEGKPYLVLGLLW 229
Cdd:cd21225    75 IEEdLKIRVQGIGAEDFVDNNKKLILGLLW 104
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 391-502 4.89e-04

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: 40.05  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 391 EGETREERTFRNWMNS--LGVNP--RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklggnmkKLENCNYA 463
Cdd:cd21241     1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGTKLLALLEVLsgeKLPCEKGRRLKRVH--------FLSNINTA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2582814608 464 VDL--GKnqaKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:cd21241    73 LKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 252-373 5.18e-04

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


Pssm-ID: 409181  Cd Length: 115  Bit Score: 39.93  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 252 LREGESLEDlmklspeELLLRWANYHLENAG-CTKITNFS-TDIKDSKAYYHLLEQVAPKGdeegIPAVVIDMSGLREKD 329
Cdd:cd21332     2 LGEGEKVND-------EIIIKWVNQTLANANkTTSITSFKdKSISTSLPVLDLIDAIAPNA----IREEMVKREDLSDAD 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2582814608 330 DIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 373
Cdd:cd21332    71 KLNNAKYAISVARKIGARVYALPEDLVEVKPKMVMTVFACLMGK 114
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 396-501 5.67e-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: 40.73  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 396 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYEKiKVP--VD---WNRVNKPPYpklggnmKKLEN 459
Cdd:cd21292    25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINL-SVPdtIDeraINKKKLTVF-------TIHEN 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2582814608 460 CNYAVdlgkNQAKF---SLVGIAGQDLNEGNRTLTLALVWQLMRR 501
Cdd:cd21292    97 LTLAL----NSASAigcNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 15-78 5.69e-04

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.88  E-value: 5.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2582814608  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:cd15897    73 QEIFRTYDTDGSGTIDSNELRQALSGA-----GYRLSEQTYDIIIRRYDRGRGNIDFDDFIQCC 131
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 13-40 6.20e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.36  E-value: 6.20e-04
                           10        20
                   ....*....|....*....|....*...
gi 2582814608   13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 6-79 7.32e-04

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 39.18  E-value: 7.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2582814608    6 VSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:smart00027   4 ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLP------QTLLAKIWNLADIDNDGELDKDEFALAMH 71
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 518-619 1.06e-03

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 39.18  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQKSSSIASF-KDpkISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKlnnAKYAISMARKIGAR 596
Cdd:cd21295    14 EEILLRWVNYHLERAGCDRRIKNFsGD--IKDSEAYTHLLKQIAPKDAGVDTSALRESDLLQR---AELMLQNADKIGCR 88

                          90       100
                  ....*....|....*....|...
gi 2582814608 597 VYALPEDLVEVNPKMVMTVFACL 619
Cdd:cd21295    89 KFVTPKDVVTGNPKLNLAFVANL 111
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 122-232 1.33e-03

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: 39.64  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFtiqENLNLALNSA 201
Cdd:cd21316    54 QKKTFTKWVNS---------HLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 202 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21316   122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-44 1.88e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLP 44
Cdd:COG5126   104 EADELFARLDTDGDGKISFEEFVAAVRDYYTP 135
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 270-370 1.90e-03

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


Pssm-ID: 409150  Cd Length: 107  Bit Score: 38.42  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 270 LLRWANYHLENAG-CTKITNFSTD-IKDSKAYYHLLEQVAPKgdeegipavVIDMS----GLREKDDIQRAECMLQQAER 343
Cdd:cd21301     6 IVEWANEKLKSAGkSTSISSFKDPsISTSLPILDLIDAIKPG---------SVDYSlvleGNSEEDKLSNAKYAISMARK 76

                          90       100
                  ....*....|....*....|....*..
gi 2582814608 344 LGCRQFVTATDVVRGNPKLNLAFIANL 370
Cdd:cd21301    77 IGARVYALPEDIVEVKPKMVMTVFACL 103
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 14-93 2.02e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 38.75  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608  14 LREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREItenLMATgDLDQDGKISFDEFIKVFHGL-KSTEVAKTFRK 92
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKL---FQEA-DTSGEDVLDEEEFVQFYNRLtKRPEIEELFKK 77


                  .
gi 2582814608  93 A 93
Cdd:cd16202    78 Y 78
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 149-205 2.18e-03

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. 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: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 38.47  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608 149 NTDDLFNAVGDGIVLCKMINLSVPDTIdeRTINKKKlTPFTIQENLNLALNSASAIG 205
Cdd:cd21208    18 PSDDFRESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 265-375 2.27e-03

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: 38.04  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 265 SPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeegipavVIDMSGLREKDDIQRAECMLQQAERL 344
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPD---------LIDMNTVAVQSNLANLEHAFYVAEKL 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2582814608 345 GCRQFVTATDVVRGNP--KLNLAFIANLFNKYP 375
Cdd:cd21239    72 GVTRLLDPEDVDVSSPdeKSVITYVSSLYDVFP 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 397-500 2.55e-03

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 37.70  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 397 ERTFRNWMNS-LGV--NPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPpypklggnMKKLENCNYAVDLGKNQ 470
Cdd:cd00014     1 EEELLKWINEvLGEelPVSITDLFESLRDGVLLCKLINKLSpgsIPKINKKPKSP--------FKKRENINLFLNACKKL 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2582814608 471 AKFSLVGIAGQDL-NEGNRTLTLALVWQLMR 500
Cdd:cd00014    73 GLPELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 267-373 2.88e-03

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


Pssm-ID: 409183  Cd Length: 112  Bit Score: 37.95  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 267 EELLLRWANYHLENAG-CTKITNFS-TDIKDSKAYYHLLEQVAPKGdeegIPAVVIDMSGLREKDDIQRAECMLQQAERL 344
Cdd:cd21334     3 DDIIVNWVNRTLSEAGkSTSIQNFKdKTISSSLAVVDLIDAIQPGC----INYDLVKTGNLTDDDKLDNAKYAVSMARKI 78

                          90       100
                  ....*....|....*....|....*....
gi 2582814608 345 GCRQFVTATDVVRGNPKLNLAFIANLFNK 373
Cdd:cd21334    79 GARVYALPEDLVEVKPKMVMTVFACLMGR 107
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 15-91 2.98e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 38.78  E-value: 2.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2582814608  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVR-EITENLMATGDLDQDGKISFDEFIKVFHGLKS-TEvakTFR 91
Cdd:cd16184    70 KQVFQQFDRDRSGSIDENELHQALSQM-----GYRLSpQFVQFLVSKYDPRARRSLTLDQFIQVCVQLQSlTD---AFR 140
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 149-205 3.72e-03

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 37.35  E-value: 3.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2582814608 149 NTDDLFNAVGDGIVLCKMINLSVPDTIdeRTINKKKLtPFTIQENLNLALNSASAIG 205
Cdd:cd21210    18 AQGDLLDALKDGVVLCKLANRILPADI--RKYKESKM-PFVQMENISAFLNAARKLG 71
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 123-177 3.81e-03

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 37.39  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608 123 KYAFVNWINKALENDpdcrhvIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDE 177
Cdd:cd21203     2 RYEAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPK 50
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 4-75 4.15e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 38.35  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608   4 GSVSDEEMMEL-------REAFAKVDTDGNGYIscnELNDLFKAacLPLPGYRVREITEN-LMATGDLDQDGKISFDEFI 75
Cdd:cd16185    51 GTIDFEEFAALhqflsnmQNGFEQRDTSRSGRL---DANEVHEA--LAASGFQLDPPAFQaLFRKFDPDRGGSLGFDDYI 125
PLN02964 PLN02964
phosphatidylserine decarboxylase
 5-73 4.62e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 4.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608   5 SVSDEEMMELREAFAK-----VDTDGNGYISCNELNDLFKAAclplpGYRVR-EITENLMATGDLDQDGKISFDE 73
Cdd:PLN02964  167 SCSIEDPVETERSFARrilaiVDYDEDGQLSFSEFSDLIKAF-----GNLVAaNKKEELFKAADLNGDGVVTIDE 236
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 159-205 5.16e-03

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 36.90  E-value: 5.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2582814608 159 DGIVLCKMINLSVPDTIdeRTINKKKLtPFTIQENLNLALNSASAIG 205
Cdd:cd21207    34 DGVILCKLINILKPGSV--KKINTSKM-AFKLMENIENFLTACKGYG 77
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 18-78 5.43e-03

EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 38.92  E-value: 5.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608  18 FAKV----DTDGNGYISCNELNDLFKAACLPLPGY------RVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:cd16178     1 FAEIwqhfDADESGYIEGKELDNFFKDLLKKLGTKdtisadEVQDVKECFMSAYDVTGDGRIQIQELANII 71
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 555-613 5.84e-03

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 37.17  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608 555 LIDAIQPGSINYDLLKTE-NLDDEEKLNNAKYAISMARKIGARVYAL-PEDLVEVNPKMVM 613
Cdd:cd21217    46 LINKIVPGTIDERKLNKKkPKNIFEATENLNLALNAAKKIGCKVVNIgPQDILDGNPHLVL 106
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
 17-85 6.59e-03

Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit CAPNS1 and CAPNS2; CAPNS1, also termed calpain small subunit 1 (CSS1), or calcium-activated neutral proteinase small subunit (CANP small subunit), or calcium-dependent protease small subunit (CDPS), or calpain regulatory subunit, is a common 28-kDa regulatory calpain subunit encoded by the calpain small 1 (Capns1, also known as Capn4) gene. It acts as a binding partner to form a heterodimer with the 80 kDa calpain large catalytic subunit and is required in maintaining the activity of calpain. CAPNS1 plays a significant role in tumor progression of human cancer, and functions as a potential therapeutic target in human hepatocellular carcinoma (HCC), nasopharyngeal carcinoma (NPC), glioma, and clear cell renal cell carcinoma (ccRCC). It may be involved in regulating migration and cell survival through binding to the SH3 domain of Ras GTPase-activating protein (RasGAP). It may also modulate Akt/FoxO3A signaling and apoptosis through PP2A. CAPNS1 contains an N-terminal glycine rich domain and a C-terminal PEF-hand domain. CAPNS2, also termed calpain small subunit 2 (CSS2), is a novel tissue-specific 30 kDa calpain small subunit that lacks two oligo-Gly stretches characteristic of the N-terminal Gly-rich domain of CAPNS1. CAPNS2 acts as a chaperone for the calpain large subunit, and appears to be the functional equivalent of CAPNS1. However, CAPNS2 binds the large subunit much more weakly than CAPNS1 and it does not undergo the autolytic conversion typical of CAPNS1.


Pssm-ID: 320063 [Multi-domain]  Cd Length: 169  Bit Score: 37.80  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2582814608  17 AFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFIK-------VFHGLKSTE 85
Cdd:cd16188    78 IYKQFDTDRSGTIGSQELPGAFEAA-----GFHLNEQLYQMIIRRYSDEDGNMDFDNFISclvrldaMFRAFKSLD 148
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 122-232 6.99e-03

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: 36.70  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 122 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFNAVGDGIVLCKMIN-LSVPDTidERTINKKKLTPFTIQENLNLALNS 200
Cdd:cd21228     5 QQNTFTRWCNE---------HLKCVNKRIYNLETDLSDGLRLIALLEvLSQKRM--YKKYNKRPTFRQMKLENVSVALEF 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2582814608 201 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 232
Cdd:cd21228    74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLI 105
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 518-619 7.17e-03

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 36.77  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 518 DDIIVNWVNTTLKEAQKSSSIASF-KDPKISTSLPVLdlIDAIQPGSINYDLLKTENLddeekLNNAKYAISMARKIGAR 596
Cdd:cd21297    12 EQILLRWFNYHLKAANWPRRVSNFsKDVSDGENYTVL--LNQLAPELCSRAPLQTTDL-----LQRAEQVLQNAEKLDCR 84

                          90       100
                  ....*....|....*....|...
gi 2582814608 597 VYALPEDLVEVNPKMVMTVFACL 619
Cdd:cd21297    85 KFLTPTSLVAGNPKLNLAFVANL 107
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 18-78 7.57e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 36.58  E-value: 7.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582814608  18 FAKVDTDGNGYISCNELnDLFKAACLPLpGYRVREITEnlmaTGDLDQDGKISFDEFIKVF 78
Cdd:cd00252    51 FDNLDNNKDGKLDKREL-APFRAPLMPL-EHCARGFFE----SCDLNKDKKISLQEWLGCF 105
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 13-73 7.58e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 38.49  E-value: 7.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2582814608  13 ELREAFAKVDTDGNGYISCNELNDLFKAAC---LPLPGYRVRE-ITENLMATGDLDQDGKISFDE 73
Cdd:cd15902   182 DFEKVFEHYDKDNNGVIEGNELDALLKDLLeknKADIDKPDLEnFRDAILRACDKNKDGKIQKTE 246
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 266-360 9.94e-03

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: 36.29  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582814608 266 PEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeegipavVIDMSGLREKDDIQRAECMLQQAER-L 344
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPE---------LFKQAAIEQMDAEARLNLAFDFAEKkL 71

                          90
                  ....*....|....*.
gi 2582814608 345 GCRQFVTATDVVRGNP 360
Cdd:cd21226    72 GIPKLLEAEDVMTGNP 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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