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Conserved domains on  [gi|961011086|ref|XP_014821657|]
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PREDICTED: plastin-2 [Calidris pugnax]

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 ...
 95-239 2.43e-102

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: 306.90  E-value: 2.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEI 239
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 248-372 7.53e-94

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: 284.16  E-value: 7.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 248 LLREGESLEDLMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAITIDMSGLREKDD 327
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 328 VQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 372
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 371-504 2.50e-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: 283.43  E-value: 2.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 371 YPALHKPENQDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 450
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 451 MKKLENCNYAVELGKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 508-622 9.46e-82

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: 252.60  E-value: 9.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 508 GGGEKVNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAISMA 587
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 961011086 588 RKIGARVYALPEDLVEVKPKMVMTVFACLMGKGMK 622
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 14-76 1.15e-07

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: 48.70  E-value: 1.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961011086  14 ELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 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 ...
 95-239 2.43e-102

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: 306.90  E-value: 2.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEI 239
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 248-372 7.53e-94

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: 284.16  E-value: 7.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 248 LLREGESLEDLMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAITIDMSGLREKDD 327
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 328 VQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 372
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 371-504 2.50e-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: 283.43  E-value: 2.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 371 YPALHKPENQDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 450
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 451 MKKLENCNYAVELGKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
7-617 1.42e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 274.13  E-value: 1.42e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   7 FSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGyKARELIQNLTTTGEGRISFDEFISI-FQNLKSDDVAK 85
Cdd:COG5069   18 TNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYN-ETPETRIHVMENVSGRLEFIKGKGVkLFNIGPQDIVD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  86 SFRKQInkkegicaIGGTSEQSSAGTQHSYSEEEKyaFVNWINKALEKDPDCKHVVPmNPETDDLFQAVGDGIVLCKMIN 165
Cdd:COG5069   97 GNPKLI--------LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 166 FSVPDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIEIS 240
Cdd:COG5069  166 DSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 241 RNEaLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEgiPAITIDMs 320
Cdd:COG5069  242 LHR-VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA--PLETTDL- 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 321 glrekddVQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPALHKPENQ---DIDWSSIEGEtREERTF 397
Cdd:COG5069  317 -------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEEEekpEIEEFDAEGE-FEARVF 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 398 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVELGKNQAkFSLVG 474
Cdd:COG5069  385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 475 IAGQDLNEGNRtLTLALIWQLMRRYTLNILEDIGGGEK-VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMP-VLDL 552
Cdd:COG5069  464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCgLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086 553 IDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVKPKM-VMTVFACLM 617
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 ...
 508-622 9.46e-82

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: 252.60  E-value: 9.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 508 GGGEKVNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAISMA 587
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 961011086 588 RKIGARVYALPEDLVEVKPKMVMTVFACLMGKGMK 622
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 117-232 1.12e-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: 93.12  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  117 EEEKYAFVNWINKALEKDPDCKHVvpmnpetDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKkltPFTIQENLNLALN 196
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961011086  197 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 232
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 121-231 9.47e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.07  E-value: 9.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   121 YAFVNWINKALEKDPdckhvvpmNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 200
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 961011086   201 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 231
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 261-373 3.37e-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: 88.88  E-value: 3.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  261 LSPEELLLRWANYHLENAG-CNKVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGL--REKDDVQRAECMLQQ 337
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPG---------LVDKKKLnkSEFDKLENINLALDV 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 961011086  338 AER-LGCRQF-VTATDVVRGNPKLNLAFIANLFNKYPA 373
Cdd:pfam00307  72 AEKkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 515-622 4.79e-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: 82.72  E-value: 4.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  515 DEIIVSWVNETLTAAGKDSTISSFKDSkISTSMPVLDLIDAIQPGSIKYDLLKTedlNDEEKLNNAKYAISMAR-KIGAR 593
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFTTD-LRDGLALCALLNKLAPGLVDKKKLNK---SEFDKLENINLALDVAEkKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 961011086  594 VYAL-PEDLVEVKPKMVMTVFACLMGKGMK 622
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 393-499 2.14e-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: 80.79  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  393 EERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPypklggnMKKLENCNYAVELGKN 466
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 961011086  467 QAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 395-498 2.64e-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: 2.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   395 RTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVP-VDWNRVNKPPYPklggnMKKLENCNYAVELGKNQaKF 470
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEKL-GG 74

                           90       100
                   ....*....|....*....|....*...
gi 961011086   471 SLVGIAGQDLNEGNRtLTLALIWQLMRR 498
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 265-370 1.28e-15

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: 72.73  E-value: 1.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   265 ELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKgdeeGIPAITIDMSGLREKDDvQRAECMLQQAERLGC- 343
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPG----LVDKKKVAASLSRFKKI-ENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 961011086   344 RQFVTATDVVRGnPKLNLAFIANLFNK 370
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 516-617 1.63e-14

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: 69.65  E-value: 1.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   516 EIIVSWVNETLTAAGKdSTISSFKDSkISTSMPVLDLIDAIQPGSIKYDLLkTEDLNDEEKLNNAKYAISMARKIG-ARV 594
Cdd:smart00033   1 KTLLRWVNSLLAEYDK-PPVTNFSSD-LKDGVALCALLNSLSPGLVDKKKV-AASLSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 961011086   595 YALPEDLVEvKPKMVMTVFACLM 617
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 14-76 1.15e-07

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: 48.70  E-value: 1.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961011086  14 ELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
12-76 1.25e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.79  E-value: 1.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961011086   12 MAELREAFGKVDISGNGFIHANDLTDVLKAANL--PLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgePLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-76 4.69e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.41  E-value: 4.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961011086   1 MASTAHFSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPgyKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:COG5126   57 AGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAVR 130
PTZ00183 PTZ00183
centrin; Provisional
 7-74 7.11e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.52  E-value: 7.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086   7 FSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISI 74
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 95-239 2.43e-102

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: 306.90  E-value: 2.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEI 239
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 ...
 95-239 6.25e-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: 295.76  E-value: 6.25e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21324    1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEI 239
Cdd:cd21324   81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 95-239 3.47e-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: 285.78  E-value: 3.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEI 239
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 248-372 7.53e-94

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: 284.16  E-value: 7.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 248 LLREGESLEDLMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAITIDMSGLREKDD 327
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 328 VQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 372
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 371-504 2.50e-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: 283.43  E-value: 2.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 371 YPALHKPENQDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGN 450
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 451 MKKLENCNYAVELGKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 95-242 6.70e-93

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: 282.72  E-value: 6.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  95 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21325    1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086 175 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEISRN 242
Cdd:cd21325   81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 380-504 1.65e-89

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: 273.02  E-value: 1.65e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 380 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNY 459
Cdd:cd21330    1 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 460 AVELGKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21330   81 AVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
7-617 1.42e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 274.13  E-value: 1.42e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   7 FSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGyKARELIQNLTTTGEGRISFDEFISI-FQNLKSDDVAK 85
Cdd:COG5069   18 TNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYN-ETPETRIHVMENVSGRLEFIKGKGVkLFNIGPQDIVD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  86 SFRKQInkkegicaIGGTSEQSSAGTQHSYSEEEKyaFVNWINKALEKDPDCKHVVPmNPETDDLFQAVGDGIVLCKMIN 165
Cdd:COG5069   97 GNPKLI--------LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 166 FSVPDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIEIS 240
Cdd:COG5069  166 DSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 241 RNEaLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEgiPAITIDMs 320
Cdd:COG5069  242 LHR-VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA--PLETTDL- 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 321 glrekddVQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPALHKPENQ---DIDWSSIEGEtREERTF 397
Cdd:COG5069  317 -------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEEEekpEIEEFDAEGE-FEARVF 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 398 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVELGKNQAkFSLVG 474
Cdd:COG5069  385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 475 IAGQDLNEGNRtLTLALIWQLMRRYTLNILEDIGGGEK-VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMP-VLDL 552
Cdd:COG5069  464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCgLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086 553 IDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVKPKM-VMTVFACLM 617
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 ...
 508-622 9.46e-82

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: 252.60  E-value: 9.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 508 GGGEKVNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAISMA 587
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 961011086 588 RKIGARVYALPEDLVEVKPKMVMTVFACLMGKGMK 622
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 387-504 3.81e-81

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: 251.06  E-value: 3.81e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 387 IEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVELGKN 466
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 961011086 467 QAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 387-504 2.19e-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: 241.37  E-value: 2.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 387 IEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVELGKN 466
Cdd:cd21298    1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 961011086 467 QaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
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 ...
 248-369 4.04e-75

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: 235.63  E-value: 4.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 248 LLREGESLEDLMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAITIDMSGLREKDD 327
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 961011086 328 VQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 369
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 251-369 7.01e-69

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: 219.07  E-value: 7.01e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 251 EGESLEDLMKLSPEELLLRWANYHLENAGCNK-VNNFSSDIKDSKAYYHLLNQVAPKGDeegipaiTIDMSGLREKDDVQ 329
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIKDSEAYTHLLKQIAPKDA-------GVDTSALRESDLLQ 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 961011086 330 RAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 369
Cdd:cd21295   74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 251-372 6.74e-67

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: 213.98  E-value: 6.74e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 251 EGESLEDLMKLSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGiPAITIDMSGLREKDDVQR 330
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFD-ENIEIDFSGFNEKNDLKR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 961011086 331 AECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 372
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 513-624 3.61e-66

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: 211.67  E-value: 3.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 513 VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAISMARKIGA 592
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 593 RVYALPEDLVEVKPKMVMTVFACLMGKGMKKV 624
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 506-620 7.06e-63

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: 203.26  E-value: 7.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 506 DIGGGEKVNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDLNDEEKLNNAKYAIS 585
Cdd:cd21332    1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 961011086 586 MARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 620
Cdd:cd21332   81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 513-620 7.56e-60

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: 194.81  E-value: 7.56e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 513 VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLKTEDlNDEEKLNNAKYAISMARKIGA 592
Cdd:cd21301    1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGN-SEEDKLSNAKYAISMARKIGA 79

                         90       100
                 ....*....|....*....|....*...
gi 961011086 593 RVYALPEDLVEVKPKMVMTVFACLMGKG 620
Cdd:cd21301   80 RVYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 389-504 7.73e-55

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: 181.71  E-value: 7.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 389 GETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKppyPKLGGNMKKLENCNYAVELGKNQ 467
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNK---PKPLNKFKKVENCNYAVDLAKKL 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961011086 468 aKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21219   78 -GFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 118-230 1.97e-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: 178.15  E-value: 1.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 118 EEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKK-LTPFTIQENLNLALN 196
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 197 SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21217   81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 513-617 8.40e-45

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: 154.74  E-value: 8.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 513 VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLkTEDLNDEEKLNNAKYAISMARKIGA 592
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLV-TEGETDEEKEQNAKYAISLARKIGA 79

                         90       100
                 ....*....|....*....|....*
gi 961011086 593 RVYALPEDLVEVKPKMVMTVFACLM 617
Cdd:cd21220   80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 119-231 1.94e-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: 1.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTIN-KKKLTPFTIQENLNLALNS 197
Cdd:cd21293    2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 198 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKI 231
Cdd:cd21293   82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 388-504 2.92e-44

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: 153.73  E-value: 2.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGEtREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIkVP--VDWNRVNKPPYPKLGGNMKKLENCNYAVELGK 465
Cdd:cd21300    4 EGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELGK 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 961011086 466 NQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21300   82 QL-GFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 113-232 3.18e-42

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: 148.36  E-value: 3.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 113 HSYSEEEKYAFVNWINKALEKDPDCKHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINK-----KKLTPFTI 187
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 188 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 232
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 253-369 4.96e-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: 147.45  E-value: 4.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 253 ESLEDLMKLSPEELLLRWANYHLENAGCNK--VNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPaitidMSGLREKDDVQR 330
Cdd:cd21218    1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDKELV-----LEVLSEEDLEKR 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 961011086 331 AECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 369
Cdd:cd21218   76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 253-369 9.15e-36

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: 129.99  E-value: 9.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 253 ESLEDLMKLSPEELLLRWANYHLENAGCN-KVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGLREKDDVQRA 331
Cdd:cd21297    1 ETLEQFLRLPPEQILLRWFNYHLKAANWPrRVSNFSKDVSDGENYTVLLNQLAPE---------LCSRAPLQTTDLLQRA 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 961011086 332 ECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFN 369
Cdd:cd21297   72 EQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 389-504 5.46e-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: 5.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 389 GETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPyPKLggNMKKLENCNYAVELGKnQ 467
Cdd:cd21299    1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPgSVNWKHANKPP-IKM--PFKKVENCNQVVKIGK-Q 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961011086 468 AKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 504
Cdd:cd21299   77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 253-368 6.38e-34

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: 124.94  E-value: 6.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 253 ESLEDLMKLSPEELLLRWANYHLENAGCNK-VNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGLREKDDVQRA 331
Cdd:cd21296    1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSDVKDAEAYAYLLNVLAPE---------HCDPATLEAKDPLERA 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961011086 332 ECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLF 368
Cdd:cd21296   72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 510-617 1.81e-32

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: 120.61  E-value: 1.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 510 GEKVNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLkTEDLNDEEKLNNAKYAISMARK 589
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLV-TPGNTEDEAYLNAKLAISIARK 79

                         90       100
                 ....*....|....*....|....*...
gi 961011086 590 IGARVYALPEDLVEVKPKMVMTVFACLM 617
Cdd:cd21303   80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 513-617 2.21e-24

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: 98.01  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 513 VNDEIIVSWVNETLTAAGKDSTISSFKDSKISTSMPVLDLIDAIQPGSIKYDLLkTEDLNDEEKLNNAKYAISMARKIGA 592
Cdd:cd21302    2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLV-TKGETDEEKRLNATYIISVARKLGC 80

                         90       100
                 ....*....|....*....|....*
gi 961011086 593 RVYALPEDLVEVKPKMVMTVFACLM 617
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 117-232 1.12e-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: 93.12  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  117 EEEKYAFVNWINKALEKDPDCKHVvpmnpetDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKkltPFTIQENLNLALN 196
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961011086  197 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 232
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 121-231 9.47e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.07  E-value: 9.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   121 YAFVNWINKALEKDPdckhvvpmNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 200
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 961011086   201 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 231
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 261-373 3.37e-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: 88.88  E-value: 3.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  261 LSPEELLLRWANYHLENAG-CNKVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGL--REKDDVQRAECMLQQ 337
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPG---------LVDKKKLnkSEFDKLENINLALDV 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 961011086  338 AER-LGCRQF-VTATDVVRGNPKLNLAFIANLFNKYPA 373
Cdd:pfam00307  72 AEKkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 515-622 4.79e-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: 82.72  E-value: 4.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  515 DEIIVSWVNETLTAAGKDSTISSFKDSkISTSMPVLDLIDAIQPGSIKYDLLKTedlNDEEKLNNAKYAISMAR-KIGAR 593
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFTTD-LRDGLALCALLNKLAPGLVDKKKLNK---SEFDKLENINLALDVAEkKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 961011086  594 VYAL-PEDLVEVKPKMVMTVFACLMGKGMK 622
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 393-499 2.14e-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: 80.79  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  393 EERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPypklggnMKKLENCNYAVELGKN 466
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 961011086  467 QAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 120-230 1.36e-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: 75.45  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 120 KYAFVNWINKALEKDPdckhvvpmNPETDDLFQAVGDGIVLCKMINFSVPDTIDErtINKKKLTPFTIQENLNLALNSAS 199
Cdd:cd00014    1 EEELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACK 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 200 AIG-CHVVNIGAEDLKEGK-PYLVLGLLWQVIK 230
Cdd:cd00014   71 KLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 395-498 2.64e-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: 2.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   395 RTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVP-VDWNRVNKPPYPklggnMKKLENCNYAVELGKNQaKF 470
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEKL-GG 74

                           90       100
                   ....*....|....*....|....*...
gi 961011086   471 SLVGIAGQDLNEGNRtLTLALIWQLMRR 498
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 265-370 1.28e-15

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: 72.73  E-value: 1.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   265 ELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKgdeeGIPAITIDMSGLREKDDvQRAECMLQQAERLGC- 343
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPG----LVDKKKVAASLSRFKKI-ENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 961011086   344 RQFVTATDVVRGnPKLNLAFIANLFNK 370
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 516-617 1.63e-14

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: 69.65  E-value: 1.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   516 EIIVSWVNETLTAAGKdSTISSFKDSkISTSMPVLDLIDAIQPGSIKYDLLkTEDLNDEEKLNNAKYAISMARKIG-ARV 594
Cdd:smart00033   1 KTLLRWVNSLLAEYDK-PPVTNFSSD-LKDGVALCALLNSLSPGLVDKKKV-AASLSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 961011086   595 YALPEDLVEvKPKMVMTVFACLM 617
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 116-230 4.26e-14

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 68.85  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 116 SEEEKyAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKK-LTPFTIQENLNLA 194
Cdd:cd21219    3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKpLNKFKKVENCNYA 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 961011086 195 LNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21219   71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 117-229 5.07e-12

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: 62.69  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 117 EEEKYAFVNWINKALEkdpdckhvvPMNPETDDLFQAVGDGIVLCKMInfsvpDTIDERTI---NKKKLTPFTIQENLNL 193
Cdd:cd21227    3 EIQKNTFTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALV-----EILQGRKLgrvIKKPLNQHQKLENVTL 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 961011086 194 ALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21227   69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 393-499 1.01e-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: 61.65  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNS-LGVNPR-VNHLYSDLSDALVIFQLYEKIkvpvdwNRVNKPPY---PKLggNMKKLENCNYAVELGKNQ 467
Cdd:cd21215    5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIKSR 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 468 aKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21215   77 -GVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 393-498 2.17e-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: 58.46  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGKNQAKF 470
Cdd:cd21193   17 QKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIIS----GEKLGKPNRGRL--RVQKIENVNKALAFLKTKVRL 90

                         90       100
                 ....*....|....*....|....*...
gi 961011086 471 SLVGiaGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21193   91 ENIG--AEDIVDGNPRLILGLIWTIILR 116
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 388-498 2.63e-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: 58.88  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGK 465
Cdd:cd21318   34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLS----GEQLPKPTRGRM--RIHSLENVDKALQFLK 107

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 466 NQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21318  108 EQ-RVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 388-498 4.13e-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: 57.38  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGK 465
Cdd:cd21246   12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGKM--RIHCLENVDKALQFLK 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 466 NQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21246   86 EQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 119-229 9.03e-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: 56.54  E-value: 9.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKdpdckhvvpMNPETDDLFQAVGDGIVLCKMINFSVPDTIDErtINKKKLTPFTIqENLNLALNSA 198
Cdd:cd21193   17 QKKTFTKWINSFLEK---------ANLEIGDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAiGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21193   85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 119-229 1.50e-09

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: 55.61  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdCKHVVpmnpetDDLFQAVGDGIVLCKMINFsvpdTIDERTINKKKLTPFTIQENLNLALNSA 198
Cdd:cd21242    6 QKRTFTNWINSQLAKHS-PPSVV------SDLFTDIQDGHRLLDLLEV----LSGQQLPREKGHNVFQCRSNIETALSFL 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21242   75 KNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 119-238 1.75e-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: 55.46  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALekdpdCKHVVPMnpETDDLFQAVGDGIVLCKMINFSVPDTID-ERTINKKKLTPFTiqeNLNLALNS 197
Cdd:cd21241    6 QKKTFTNWINSYL-----AKRKPPM--KVEDLFEDIKDGTKLLALLEVLSGEKLPcEKGRRLKRVHFLS---NINTALKF 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 961011086 198 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIkigLFADIE 238
Cdd:cd21241   76 LESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 388-498 3.02e-09

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: 55.45  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS-LG-VNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGK 465
Cdd:cd21317   27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLS----GEQLPKPTKGRM--RIHCLENVDKALQFLK 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 466 NQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21317  101 EQ-KVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 117-233 5.61e-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: 54.35  E-value: 5.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 117 EEEKYAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKK----LTPFTIQENLN 192
Cdd:cd21300    6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 961011086 193 LALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGL 233
Cdd:cd21300   75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHI 115
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 116-230 6.34e-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: 54.16  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 116 SEEEKyAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINK---KKLTPFTIQENLN 192
Cdd:cd21298    5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 961011086 193 LALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21298   73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 119-230 1.05e-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: 53.17  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdckhvVPMNPETDDLfqavGDGIVLCKMInfsvpDTIDERTINKKKLTP-FTIQ--ENLNLAL 195
Cdd:cd21215    5 QKKTFTKWLNTKLSSRG-----LSITDLVTDL----SDGVRLIQLL-----EIIGDESLGRYNKNPkMRVQklENVNKAL 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 961011086 196 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21215   71 EFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 372-503 1.07e-08

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: 53.88  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 372 PALHKPENQDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLGG 449
Cdd:cd21310    1 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLS----QKKMYRKYHPRPNF 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 450 NMKKLENCNYAVELgKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 503
Cdd:cd21310   72 RQMKLENVSVALEF-LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 388-502 1.27e-08

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: 53.83  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVE- 462
Cdd:cd21236   13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL---------SGDTLPREKGRMRfhRLQNVQIALDy 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 961011086 463 LGKNQAKfsLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 502
Cdd:cd21236   84 LKRRQVK--LVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 515-610 1.30e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 53.07  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 515 DEIIVSWVNETLTAAGKD-STISSF----KDSKISTSmpvldLIDAIQPGSIKyDLLKTEDLNDEEKLNNAKYAISMARK 589
Cdd:cd21218   12 EEILLRWVNYHLKKAGPTkKRVTNFssdlKDGEVYAL-----LLHSLAPELCD-KELVLEVLSEEDLEKRAEKVLQAAEK 85

                         90       100
                 ....*....|....*....|.
gi 961011086 590 IGARVYALPEDLVEVKPKMVM 610
Cdd:cd21218   86 LGCKYFLTPEDIVSGNPRLNL 106
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 372-503 4.09e-08

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: 52.40  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 372 PALHKPENQDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKlgg 449
Cdd:cd21308    5 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR--- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 450 nMKKLENCNYAVELgKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 503
Cdd:cd21308   77 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 393-493 7.59e-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: 50.86  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVELGKNQa 468
Cdd:cd21188    4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL---------SGESLPRERGRMRfhRLQNVQTALDFLKYR- 73

                         90       100
                 ....*....|....*....|....*
gi 961011086 469 KFSLVGIAGQDLNEGNRTLTLALIW 493
Cdd:cd21188   74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 119-238 9.18e-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: 50.65  E-value: 9.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKdpdckHVVPMNpeTDDLFQAVGDGIVLCKMINFSVPDTIDERTinKKKLTPFTIQENLNLALNSA 198
Cdd:cd21190    6 QKKTFTNWINSHLAK-----LSQPIV--INDLFVDIKDGTALLRLLEVLSGQKLPIES--GRVLQRAHKLSNIRNALDFL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIkigLFADIE 238
Cdd:cd21190   77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 372-503 1.11e-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: 51.23  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 372 PALHKPENQDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKlgg 449
Cdd:cd21309    2 PVTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFR--- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961011086 450 nMKKLENCNYAVELgKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 503
Cdd:cd21309   74 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 14-76 1.15e-07

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: 48.70  E-value: 1.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961011086  14 ELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
12-76 1.25e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.79  E-value: 1.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961011086   12 MAELREAFGKVDISGNGFIHANDLTDVLKAANL--PLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgePLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 393-499 1.45e-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: 50.17  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPVDWNRvnKPPYPKlggnmKKLENCNYAVELgKNQ 467
Cdd:cd21183    5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLstrPLKRSYNR--RPAFQQ-----HYLENVSTALKF-IEA 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 468 AKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21183   77 DHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 407-497 1.58e-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: 49.88  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 407 NPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPyPKlgGNMKKLENCNYAVElGKNQAKFSLVGIAGQDLNEGN 484
Cdd:cd21217   27 DPDGDDLFEALRDGVLLCKLINKIV-PgtIDERKLNKKK-PK--NIFEATENLNLALN-AAKKIGCKVVNIGPQDILDGN 101

                         90
                 ....*....|...
gi 961011086 485 RTLTLALIWQLMR 497
Cdd:cd21217  102 PHLVLGLLWQIIR 114
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 388-498 1.77e-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: 51.20  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGK 465
Cdd:cd21316   49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 466 NQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21316  123 EQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 119-229 2.74e-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: 49.32  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdcKHVVpmnpetdDLFQAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 198
Cdd:cd21188    4 QKKTFTKWVNKHLIKAR--RRVV-------DLFEDLRDGHNLISLLEVLSGESLPR----ERGRMRFHRLQNVQTALDFL 70

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21188   71 KYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-76 4.69e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.41  E-value: 4.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961011086   1 MASTAHFSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPgyKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:COG5126   57 AGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAVR 130
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 393-499 5.00e-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: 48.44  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPklggnMKKLENCNYAVELGKNQAkF 470
Cdd:cd21227    5 QKNTFTNWVNEQlkPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQ-----HQKLENVTLALKAMAEDG-I 78

                         90       100
                 ....*....|....*....|....*....
gi 961011086 471 SLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21227   79 KLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 515-616 6.04e-07

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: 48.73  E-value: 6.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 515 DEIIVSWVNETLTAAGKdSTISSFKdSKISTSMPVLDLIDAIQPGSIKYDLLKTEDL---NDEEKLNNAKYAISMARKIG 591
Cdd:cd21326   14 EELLLRWVNYHLTNAGW-QNISNFS-QDIKDSRAYFHLLNQIAPKGDVFDENIEIDFsgfNEKNDLKRAEYMLQEADKLG 91

                         90       100
                 ....*....|....*....|....*
gi 961011086 592 ARVYALPEDLVEVKPKMVMTVFACL 616
Cdd:cd21326   92 CRQFVTPADVVSGNPKLNLAFVANL 116
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 388-502 8.12e-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: 48.11  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYE---KIKVPVDWNRVNkppypklggnMKKLENCNYAVE 462
Cdd:cd21237    2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEvlsGVKLPREKGRMR----------FHRLQNVQIALD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 961011086 463 LGKnQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 502
Cdd:cd21237   72 FLK-QRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 393-499 8.48e-07

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: 47.87  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwNRVNKPPYPKLGGNMKKLENCNYAVELGKNQaKF 470
Cdd:cd21228    5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQ----KRMYKKYNKRPTFRQMKLENVSVALEFLERE-SI 79

                         90       100
                 ....*....|....*....|....*....
gi 961011086 471 SLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21228   80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 390-499 1.05e-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: 47.53  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 390 ETREERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKvpvdwNRVNKPPYPKLGGN-MKKLENCNYAVELGK 465
Cdd:cd21225    2 EKVQIKAFTAWVNSVLEKrgiPKISDLATDLSDGVRLIFFLELVS-----GKKFPKKFDLEPKNrIQMIQNLHLAMLFIE 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 466 NQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21225   77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 119-229 1.14e-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: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdcKHVvpmnpetDDLFQAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 198
Cdd:cd21236   18 QKKTFTKWINQHLMKVR--KHV-------NDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21236   85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 380-503 1.20e-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: 47.83  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 380 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnRVNKPPypklggNMK-- 452
Cdd:cd21311    8 EDAQWKRIQ-----QNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsq 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 961011086 453 KLENCNYAVELGKNQAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 503
Cdd:cd21311   73 KLENVSVALKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISM 123
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 119-240 1.39e-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: 47.71  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 198
Cdd:cd21235    7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEIS 240
Cdd:cd21235   74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 15-89 1.40e-06

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: 47.99  E-value: 1.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961011086  15 LREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQNL-KSDDVAKSFRK 89
Cdd:cd16202    2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRLtKRPEIEELFKK 77
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 391-499 1.51e-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: 47.45  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 391 TREERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnrvnKPPYPKLggNMKKLENCNYAVEL 463
Cdd:cd21247   19 TMQKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELIsgeQLP-------RPSRGKM--RVHFLENNSKAITF 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 961011086 464 GKNQAKFSLVGiaGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21247   90 LKTKVPVKLIG--PENIVDGDRTLILGLIWIIILRF 123
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 393-496 2.08e-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: 46.54  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMN---SLGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVELgKNQ 467
Cdd:cd21232    3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGL---------TGKSLPKERGSTRvhALNNVNRVLQV-LHQ 72

                         90       100
                 ....*....|....*....|....*....
gi 961011086 468 AKFSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21232   73 NNVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 388-511 2.24e-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: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVEL 463
Cdd:cd21235    2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 961011086 464 GKNQaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNILEDIGGGE 511
Cdd:cd21235   73 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 119-229 3.12e-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: 46.94  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdCKhvvpmnpeTDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 198
Cdd:cd21318   39 QKKTFTKWVNSHLARVP-CR--------INDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21318  107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 393-493 3.83e-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: 45.84  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGGNMK--KLENCNYAVE-LGKN 466
Cdd:cd21186    3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVL---------TGKKLKPEKGRMRvhHLNNVNRALQvLEQN 73

                         90       100
                 ....*....|....*....|....*..
gi 961011086 467 QAKfsLVGIAGQDLNEGNRTLTLALIW 493
Cdd:cd21186   74 NVK--LVNISSNDIVDGNPKLTLGLVW 98
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 119-229 4.04e-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: 45.93  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMINFsVPDTIDERTINKKKLTPFTIQENLNLALNSA 198
Cdd:cd21183    5 QANTFTRWCNE---------HLKERGMQIHDLATDFSDGLCLIALLEN-LSTRPLKRSYNRRPAFQQHYLENVSTALKFI 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21183   75 EADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 116-230 5.06e-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: 45.96  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 116 SEEEKyAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQENLNLA 194
Cdd:cd21299    3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 961011086 195 LNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21299   71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 119-225 6.77e-06

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: 45.27  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPDCKHVVpmnpetdDLFQAVGDGIVLCKMINFSVPDTIDErtINKKKLTPFTIQENLNLALNSA 198
Cdd:cd21212    1 EIEIYTDWANHYLEKGGHKRIIT-------DLQKDLGDGLTLVNLIEAVAGEKVPG--IHSRPKTRAQKLENIQACLQFL 71

                         90       100
                 ....*....|....*....|....*..
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLL 225
Cdd:cd21212   72 AALGVDVQGITAEDIVDGNLKAILGLF 98
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 390-496 8.74e-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: 44.69  E-value: 8.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 390 ETREERTFRNWMNSL--GVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLggNMKKLENCNYAVELGKNQ 467
Cdd:cd21214    3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVIS----GERLPKPERGKM--RFHKIANVNKALDFIASK 76

                         90       100
                 ....*....|....*....|....*....
gi 961011086 468 AkFSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21214   77 G-VKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 116-230 9.54e-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: 44.98  E-value: 9.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 116 SEEEKyAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMINFS-VPdtIDERTINKKkltPFTIQ------ 188
Cdd:cd21329    5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTrVP--VDWGHVNKP---PYPALggnmkk 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 961011086 189 -ENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21329   68 iENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 404-498 1.26e-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: 45.13  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 404 LGVNPRVNHLYSDLSDALVIFQLYEKIkVP--VDWNRVNKPPYP-KLGGNMKKLENCNYAVELGKNQAkFSLVGIAGQDL 480
Cdd:cd21294   29 LPFPTDTFQLFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKnKPLNNFQMIENNNIVINSAKAIG-CSVVNIGAGDI 106

                         90
                 ....*....|....*...
gi 961011086 481 NEGNRTLTLALIWQLMRR 498
Cdd:cd21294  107 IEGREHLILGLIWQIIRR 124
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 388-496 1.43e-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: 44.53  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVpvdwnrvNKPPYPKLGGNMKKLENCNYAVE-L 463
Cdd:cd21231    2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-------QKLVKEKGSTRVHALNNVNKALQvL 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 464 GKNQAkfSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21231   75 QKNNV--DLVNIGSADIVDGNHKLTLGLIWSII 105
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 119-229 1.94e-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: 44.11  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKdpdCkhvvpmNP--ETDDLFQAVGDGIVLCKMIN-FSVPDTIDERTINKKKLtpFTIQeNLNLAL 195
Cdd:cd21191    6 QKRTFTRWINLHLEK---C------NPplEVKDLFVDIQDGKILMALLEvLSGQNLLQEYKPSSHRI--FRLN-NIAKAL 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 196 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21191   74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 118-229 2.06e-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: 43.92  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 118 EEKYAFVNWINKALEKdpdckhvvpMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERtiNKKKLTPFTIQeNLNLALNS 197
Cdd:cd21214    5 QQRKTFTAWCNSHLRK---------AGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIA-NVNKALDF 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 198 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21214   73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 262-357 2.14e-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: 43.76  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 262 SPEELLLRWANYHLENAgcnKVNNFSSDIKDSKAYYHLLNQVAPkgdeeGIPAITIDMSglrEKDDVQRAECMLQQAER- 340
Cdd:cd21184    1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKP-----GLIPDNESLD---KENPLENATKAMDIAEEe 69

                         90
                 ....*....|....*..
gi 961011086 341 LGCRQFVTATDVVRGNP 357
Cdd:cd21184   70 LGIPKIITPEDMVSPNV 86
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 119-229 2.77e-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: 43.89  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 198
Cdd:cd21246   17 QKKTFTKWVNS---------HLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCL---ENVDKALQFL 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21246   85 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 388-496 3.65e-05

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: 43.28  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS-LGVNPR---VNHLYSDLSDALVIFQLYEKIKvpvdwnrVNKPPYPKLGGNMKKLENCNYAVEL 463
Cdd:cd21242    1 EQEQTQKRTFTNWINSqLAKHSPpsvVSDLFTDIQDGHRLLDLLEVLS-------GQQLPREKGHNVFQCRSNIETALSF 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 464 GKNQAkFSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21242   74 LKNKS-IKLINIHVPDIIEGKPSIILGLIWTII 105
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 119-230 3.76e-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: 43.84  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMIN-FSVPdtIDERTINK----------KKLtpfti 187
Cdd:cd21331   23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKppypklganmKKL----- 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 961011086 188 qENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21331   85 -ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 122-226 4.00e-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: 43.29  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 122 AFVNWINKALEKdpdcKHVVPMNPETDDLfqavGDGIvlcKMINFSvpDTIDERTINKK-KLTPFT-IQ--ENLNLALNS 197
Cdd:cd21225    8 AFTAWVNSVLEK----RGIPKISDLATDL----SDGV---RLIFFL--ELVSGKKFPKKfDLEPKNrIQmiQNLHLAMLF 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 961011086 198 ASA-IGCHVVNIGAEDLKEGKPYLVLGLLW 226
Cdd:cd21225   75 IEEdLKIRVQGIGAEDFVDNNKKLILGLLW 104
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 8-71 4.90e-05

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: 42.90  E-value: 4.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961011086   8 SEEEMAELREAFGKVDISGNGFIHANDLTDVLKAA-----NLPLPGYKARELIQNLTTTGEGRISFDEF 71
Cdd:cd16252   32 SEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVpssmpVAPLSDEEAEAMIQAADTDGDGRIDFQEF 100
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 119-229 5.25e-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: 42.99  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKdpdckhvvPMNPETDDLFQAVGDGIVLCKMINfsvpDTIDERTINKKKLTPFTIQENLNLALNSA 198
Cdd:cd21231    7 QKKTFTKWINAQFAK--------FGKPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21231   75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 516-611 5.96e-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: 42.22  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 516 EIIVSWVNETLTaagkDSTISSFkDSKISTSMPVLDLIDAIQPGSIKYdllkTEDLNDEEKLNNAKYAISMA-RKIGARV 594
Cdd:cd21184    4 SLLLEWVNSKIP----EYKVKNF-TTDWNDGKALAALVDALKPGLIPD----NESLDKENPLENATKAMDIAeEELGIPK 74

                         90
                 ....*....|....*....
gi 961011086 595 YALPEDLV--EVKPKMVMT 611
Cdd:cd21184   75 IITPEDMVspNVDELSVMT 93
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 262-372 6.66e-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: 42.38  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 262 SPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGLREKDDVQRAECMLQQAER- 340
Cdd:cd21189    1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPD---------LIDFRSVRNQSNRENLENAFNVAEKe 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 341 LGCRQFVTATDVVRGNP--KLNLAFIANLFNKYP 372
Cdd:cd21189   72 FGVTRLLDPEDVDVPEPdeKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 119-240 6.98e-05

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: 42.71  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMInfSVPDTIdeRTINKKKLTPFTIQENLNLALNSA 198
Cdd:cd21237    7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISLL--EVLSGV--KLPREKGRMRFHRLQNVQIALDFL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEIS 240
Cdd:cd21237   74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
PTZ00183 PTZ00183
centrin; Provisional
 7-74 7.11e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.52  E-value: 7.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086   7 FSEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISI 74
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 388-496 8.46e-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: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNSL--GVNP--RVNHLYSDLSDALVIFQLYEKIKvpvDWNRVNKppYPKLGGNMKKLENCNYAVEL 463
Cdd:cd21191    1 ERENVQKRTFTRWINLHleKCNPplEVKDLFVDIQDGKILMALLEVLS---GQNLLQE--YKPSSHRIFRLNNIAKALKF 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 464 GKNQaKFSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21191   76 LEDS-NVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 251-372 8.55e-05

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: 42.46  E-value: 8.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 251 EGESLEDLMKLSPEELLLRWANYHLENagcNKVNNFSSDIKDSKAYYHLLNQVApkgdeegiPAITIDMSGLREKDDVQR 330
Cdd:cd21315    5 EDDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALA--------PGLCPDWEDWDPKDAVKN 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 961011086 331 AECMLQQAER-LGCRQFVTATDVVrgNPKLNLAFIANLFNKYP 372
Cdd:cd21315   74 AKEAMDLAEDwLDVPQLIKPEEMV--NPKVDELSMMTYLSQFP 114
PTZ00184 PTZ00184
calmodulin; Provisional
 8-74 1.08e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.83  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961011086   8 SEEEmaeLREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISI 74
Cdd:PTZ00184  82 SEEE---IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKM 145
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 388-496 1.18e-04

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: 41.79  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS----LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKppypklggNMKKLENCNYA 460
Cdd:cd21190    1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 961011086 461 VELGKNQaKFSLVGIAGQDLNEGNRTLTLALIWQLM 496
Cdd:cd21190   73 LDFLTKR-CIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 388-499 1.38e-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: 41.59  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 388 EGETREERTFRNWMNS--LGVNP--RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklggnmkKLENCNYA 460
Cdd:cd21241    1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGTKLLALLEVLsgeKLPCEKGRRLKRVH--------FLSNINTA 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 961011086 461 VEL--GKnqaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRY 499
Cdd:cd21241   73 LKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 515-616 1.38e-04

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 41.49  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 515 DEIIVSWVNETLTAAGKDSTISSF----KDSKISTSmpvldLIDAIQPgsiKYDLLKTEDLNDEEKLNNAKYAISMARKI 590
Cdd:cd21295   14 EEILLRWVNYHLERAGCDRRIKNFsgdiKDSEAYTH-----LLKQIAP---KDAGVDTSALRESDLLQRAELMLQNADKI 85

                         90       100
                 ....*....|....*....|....*.
gi 961011086 591 GARVYALPEDLVEVKPKMVMTVFACL 616
Cdd:cd21295   86 GCRKFVTPKDVVTGNPKLNLAFVANL 111
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 515-616 1.41e-04

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: 41.88  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 515 DEIIVSWVNETLTAAGKdSTISSFKdSKISTSMPVLDLIDAIQPGSIKYDLLKTE----DLNDEEKLNNAKYAISMARKI 590
Cdd:cd21328   17 EELLLRWANFHLENAGW-QKINNFS-SDIKDSRAYFHLLNQIAPKGQKEGEPRIDinmsGFNEKDDLKRAEYMLQQADKL 94

                         90       100
                 ....*....|....*....|....*.
gi 961011086 591 GARVYALPEDLVEVKPKMVMTVFACL 616
Cdd:cd21328   95 GCRQFVTPADVVSGNPKLNLAFVANL 120
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 119-229 2.12e-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: 41.58  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 198
Cdd:cd21317   32 QKKTFTKWVNS---------HLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21317  100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 119-229 2.55e-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: 40.83  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdckhvvpmNPETDDLFQAVGDGIVLCKMInfsvpDTIDERTINKKK-LTPFTIQENLNLALNS 197
Cdd:cd21186    3 QKKTFTKWINSQLSKAN--------KPPIKDLFEDLRDGTRLLALL-----EVLTGKKLKPEKgRMRVHHLNNVNRALQV 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 198 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21186   70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 264-369 2.96e-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: 40.40  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 264 EELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGLREKDDVQRAE---CMLQQAER 340
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPG---------SIPKINKKPKSPFKKREninLFLNACKK 71

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 341 LGC--RQFVTATDVV-RGNPKLNLAFIANLFN 369
Cdd:cd00014   72 LGLpeLDLFEPEDLYeKGNLKKVLGTLWALAL 103
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 393-498 2.98e-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: 41.50  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 393 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYEKiKVP--VD---WNRVNKPPYpklggnmKKLEN 456
Cdd:cd21292   25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINL-SVPdtIDeraINKKKLTVF-------TIHEN 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961011086 457 CNYAVelgkNQAKF---SLVGIAGQDLNEGNRTLTLALIWQLMRR 498
Cdd:cd21292   97 LTLAL----NSASAigcNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 119-230 3.34e-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: 40.74  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckhvVPMNPETDDLFQAVGDGIVLCKMI-NFSVPdtIDERTINK----------KKLtpfti 187
Cdd:cd21330   14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 961011086 188 qENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 230
Cdd:cd21330   76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 123-226 5.90e-04

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 39.63  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 123 FVNWINKALEKDpDCKHVVpmnpetDDLFQAVGDGIVLCKMINFSVPDTIDErtINKKKLTPFTIQENLNLALNSASAIG 202
Cdd:cd21286    5 YTDWANHYLAKS-GHKRLI------KDLQQDIADGVLLAEIIQIIANEKVED--INGCPRSQSQMIENVDVCLSFLAARG 75

                         90       100
                 ....*....|....*....|....
gi 961011086 203 CHVVNIGAEDLKEGKPYLVLGLLW 226
Cdd:cd21286   76 VNVQGLSAEEIRNGNLKAILGLFF 99
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 270-367 6.67e-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: 39.49  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 270 WANYHLENAGCNK-VNNFSSDIKDSKAYYHLLNQVApkgdEEGIPAITidmsgLREKDDVQRAE----CmLQQAERLGCR 344
Cdd:cd21212    8 WANHYLEKGGHKRiITDLQKDLGDGLTLVNLIEAVA----GEKVPGIH-----SRPKTRAQKLEniqaC-LQFLAALGVD 77

                         90       100
                 ....*....|....*....|....
gi 961011086 345 -QFVTATDVVRGNPKLNLAFIANL 367
Cdd:cd21212   78 vQGITAEDIVDGNLKAILGLFFSL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 516-616 9.50e-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: 38.86  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 516 EIIVSWVNETLtAAGKDSTISSFKDSkISTSMPVLDLIDAIQPGSIKYDllKTEDLNDEEKLNNAKYAISMARKIGARVY 595
Cdd:cd00014    2 EELLKWINEVL-GEELPVSITDLFES-LRDGVLLCKLINKLSPGSIPKI--NKKPKSPFKKRENINLFLNACKKLGLPEL 77

                         90       100
                 ....*....|....*....|....
gi 961011086 596 AL--PEDLVEVK-PKMVMTVFACL 616
Cdd:cd00014   78 DLfePEDLYEKGnLKKVLGTLWAL 101
PTZ00184 PTZ00184
calmodulin; Provisional
 8-77 9.60e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.13  E-value: 9.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086   8 SEEEMAELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQN 77
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMAR 75
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 13-76 1.07e-03

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: 38.67  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961011086  13 AELREAFGKVDISGNGFIHANDLTDVLK---AANLPLPGYKARELIQNLTTTGEGRISFDEFISIFQ 76
Cdd:cd16251   34 DQIKKVFQILDKDKSGFIEEEELKYILKgfsIAGRDLTDEETKALLAAGDTDGDGKIGVEEFATLVA 100
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 14-71 1.09e-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: 40.28  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961011086  14 ELREAFGKVDISGNGFIHANDLTDVLKAANLPLPGYKARELIQNLTTTGEGRISFDEF 71
Cdd:cd16185    1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEF 58
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 119-229 1.13e-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: 40.03  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKalekdpdckHVVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFtiqENLNLALNSA 198
Cdd:cd21316   54 QKKTFTKWVNS---------HLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 199 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21316  122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 14-97 1.22e-03

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: 39.90  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086  14 ELREAFGKVDISGNGFIHANDLTDVLKAAnlplpGYK-ARELIQNLTT---TGEGRISFDEFISIFQNLKSddVAKSFRK 89
Cdd:cd16182   73 KWQAIFKKFDTDRSGTLSSYELRKALESA-----GFHlSNKVLQALVLryaDSTGRITFEDFVSCLVRLKT--AFETFSA 145


                 ....*...
gi 961011086  90 QINKKEGI 97
Cdd:cd16182  146 LDKKNEGV 153
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 394-497 1.42e-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: 38.47  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 394 ERTFRNWMNS-LGV--NPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPpypklggnMKKLENCNYAVELGKNQ 467
Cdd:cd00014    1 EEELLKWINEvLGEelPVSITDLFESLRDGVLLCKLINKLSpgsIPKINKKPKSP--------FKKRENINLFLNACKKL 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 961011086 468 AKFSLVGIAGQDL-NEGNRTLTLALIWQLMR 497
Cdd:cd00014   73 GLPELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 261-372 1.42e-03

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: 38.48  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 261 LSPEELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKgdeegipaiTIDMSGLREKDDVQRAECMLQQAER 340
Cdd:cd21240    3 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPD---------LVDMERVQIQSNRENLEQAFEVAER 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 961011086 341 LGCRQFVTATDVVRGNP--KLNLAFIANLFNKYP 372
Cdd:cd21240   74 LGVTRLLDAEDVDVPSPdeKSVITYVSSIYDAFP 107
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 146-202 1.53e-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: 38.86  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961011086 146 ETDDLFQAVGDGIVLCKMINFSVPDTIdeRTINKKKlTPFTIQENLNLALNSASAIG 202
Cdd:cd21208   18 PSDDFRESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 120-174 1.96e-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: 38.16  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961011086 120 KYAFVNWINKALEKDpdckhvVPMNPETDDLFQAVGDGIVLCKMINFSVPDTIDE 174
Cdd:cd21203    2 RYEAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPK 50
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 264-368 2.33e-03

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: 38.02  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 264 EELLLRWANYHLENAG-CNKVNNFSS-DIKDSKAYYHLLNQVAPKgdeegipAITIDM--SGLREKDDVQRAECMLQQAE 339
Cdd:cd21220    3 DADILAWANSKVREAGkSSPISSFKDpSLSTGLFLLDLLAAIDPG-------AVDYDLvtEGETDEEKEQNAKYAISLAR 75

                         90       100
                 ....*....|....*....|....*....
gi 961011086 340 RLGCRQFVTATDVVRGNPKLNLAFIANLF 368
Cdd:cd21220   76 KIGAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 249-370 3.37e-03

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: 37.62  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 249 LREGESLEDlmklspeELLLRWANYHLENAgcNKVNNFSS----DIKDSKAYYHLLNQVAPKGDEEGIpaitIDMSGLRE 324
Cdd:cd21332    2 LGEGEKVND-------EIIIKWVNQTLANA--NKTTSITSfkdkSISTSLPVLDLIDAIAPNAIREEM----VKREDLSD 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 961011086 325 KDDVQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 370
Cdd:cd21332   69 ADKLNNAKYAISVARKIGARVYALPEDLVEVKPKMVMTVFACLMGK 114
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 119-229 4.70e-03

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: 37.30  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 119 EKYAFVNWINKALEKDPdckhvvpmNPETDDLFQAVGDGIVLCKMInfsvpDTIDERTINKKK-LTPFTIQENLNLALNS 197
Cdd:cd21232    3 QKKTFTKWINARFSKSG--------KPPIKDMFTDLRDGRKLLDLL-----EGLTGKSLPKERgSTRVHALNNVNRVLQV 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 961011086 198 ASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 229
Cdd:cd21232   70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 264-371 6.19e-03

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: 36.74  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 264 EELLLRWANYHLENAGCNKVNNFSSDIKDSKAYYHLLNQVAPKGDEEGIPaitidmsgLREKDDVQRAE----CMLQQAE 339
Cdd:cd21225    6 IKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFD--------LEPKNRIQMIQnlhlAMLFIEE 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 961011086 340 RLGCR-QFVTATDVVRGNPKLNLAFIANLFNKY 371
Cdd:cd21225   78 DLKIRvQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 515-616 7.56e-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: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011086 515 DEIIVSWVNETLTAAGKDSTISSF-KDSKISTSMPVLdlIDAIQPGSIKYDLLKTEDLndeekLNNAKYAISMARKIGAR 593
Cdd:cd21297   12 EQILLRWFNYHLKAANWPRRVSNFsKDVSDGENYTVL--LNQLAPELCSRAPLQTTDL-----LQRAEQVLQNAEKLDCR 84

                         90       100
                 ....*....|....*....|...
gi 961011086 594 VYALPEDLVEVKPKMVMTVFACL 616
Cdd:cd21297   85 KFLTPTSLVAGNPKLNLAFVANL 107
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 156-202 8.09e-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: 36.52  E-value: 8.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 961011086 156 DGIVLCKMINFSVPDTIdeRTINKKKLtPFTIQENLNLALNSASAIG 202
Cdd:cd21207   34 DGVILCKLINILKPGSV--KKINTSKM-AFKLMENIENFLTACKGYG 77
 
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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