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Conserved domains on  [gi|1717014095|ref|XP_030064731|]
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plastin-3 isoform X1 [Microcaecilia unicolor]

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 ...
 169-313 2.20e-107

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: 321.92  E-value: 2.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIEL 313
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 445-578 6.28e-98

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: 297.30  E-value: 6.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 445 YPALTKPVNQDIDWTLLEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 524
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 525 MKKLENCNYAVDLGKYPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 322-443 1.07e-89

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: 275.31  E-value: 1.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 322 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEERIDINMSGFSEKDD 401
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 402 LKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21328    81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 587-698 4.95e-75

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: 236.71  E-value: 4.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLMGRGMKKV 698
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 84-150 2.41e-15

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: 70.65  E-value: 2.41e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKEANLPLPgykvREIIQRLMADGDKNKDGKIGFDEFVYIFQ 150
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 169-313 2.20e-107

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: 321.92  E-value: 2.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIEL 313
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 445-578 6.28e-98

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: 297.30  E-value: 6.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 445 YPALTKPVNQDIDWTLLEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 524
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 525 MKKLENCNYAVDLGKYPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 322-443 1.07e-89

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: 275.31  E-value: 1.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 322 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEERIDINMSGFSEKDD 401
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 402 LKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21328    81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
53-691 1.36e-87

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 286.84  E-value: 1.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  53 LEENKLvsQRYYTSQFHKMANTAQISKDEleelrEAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLmadg 132
Cdd:COG5069     1 MEAKKW--QKVQKKTFTKWTNEKLISGGQ-----KEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVM---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 133 dKNKDGKIGFDEFV--YIFQELKSsDIAKTFRKAInrkegicaIGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPD 210
Cdd:COG5069    70 -ENVSGRLEFIKGKgvKLFNIGPQ-DIVDGNPKLI--------LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDED 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 211 CQHVLPmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAE 285
Cdd:COG5069   138 TGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIP 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 286 DLKAgkpHLVLgLLWQIIKIGLFADIELSKNEaLAALLRDGETLEDlMKLSPEELLLRWAN-FHLENAGWNkINNFSSDI 364
Cdd:COG5069   217 DERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK-VVNFSKDV 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 365 KDSRAYFHLLNQIAPKGQKEGEERIDInmsgfsekddLKRAEYMLQQADRLGCRQFVTPAdvvsGNPKLNLAFVANLFNK 444
Cdd:COG5069   290 SDGENYTDLLNQLNALCSRAPLETTDL----------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNT 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 445 YPALtKPVNQ----DIDWTLLEGEtREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVP--VDWNKVNKPPY 518
Cdd:COG5069   356 HPGQ-EPLEEeekpEIEEFDAEGE-FEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPA 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 519 PKLGAN-MKKLENCNYAVDLGKyPAKFSLVGIGGQDLNDGNStLTLALVWQLMRRYSLNVLEDLG-DGQKVNDDIIVRWV 596
Cdd:COG5069   434 SGIEENrFKAFENENYAVDLGI-TEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWL 511

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 597 NRTLAEAGKSTSIQSFKDKTISTSWA-VVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVS--MARRIGARVYALPE 673
Cdd:COG5069   512 GSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPE 591

                         650
                  ....*....|....*....
gi 1717014095 674 DLVEVKPKM-VMTVFACLM 691
Cdd:COG5069   592 DINGVRPRLdVLTFIESLM 610
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 587-698 4.95e-75

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: 236.71  E-value: 4.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLMGRGMKKV 698
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 335-447 9.70e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 96.20  E-value: 9.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 335 LSPEELLLRWANFHLENAGWNK-INNFSSDIKDSRAYFHLLNQIAPKGQKEGEERidinmsgFSEKDDLKRAEYMLQQAD 413
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrVTNFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENINLALDVAE 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 414 R-LGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 447
Cdd:pfam00307  74 KkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 191-306 1.67e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 95.82  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 191 EEEKYAFVNWINKALENDPDCQHVlpmnpntNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKkltPFTIQENLNLALN 270
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 271 SAS-AIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIG 306
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 195-305 6.35e-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: 90.84  E-value: 6.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  195 YAFVNWINKALENDPdcqhvlpmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKlTPFTIQENLNLALNSASA 274
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1717014095  275 IGCHVVNIGAEDLKAGkPHLVLGLLWQIIKI 305
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 589-696 4.50e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.10  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 589 DDIIVRWVNRTLAEAGKSTSIQSFKdKTISTSWAVVDLIDAIQPGCINYDLVKIgdlSEDDKHDNAKFAVSMARR-IGAR 667
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK---SEFDKLENINLALDVAEKkLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1717014095 668 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 696
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 467-573 5.75e-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: 80.02  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNSL----GVKPHVNHLYSDLQDALVILQLYEKIKvP--VDWNKVNKPPypklganMKKLENCNYAVDLGKY 540
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 541 PAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 339-444 1.64e-17

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: 78.13  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  339 ELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEgeeriDINMSGFSEKDDLKRAEYMLQQADRLGC- 417
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 1717014095  418 RQFVTPADVVSGnPKLNLAFVANLFNK 444
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 469-572 4.57e-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: 74.27  E-value: 4.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  469 RTFRNWMNSLGVK---PHVNHLYSDLQDALVILQLYEKIKVP-VDWNKVNKPPYPklganMKKLENCNYAVDLGKyPAKF 544
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74

                           90       100
                   ....*....|....*....|....*...
gi 1717014095  545 SLVGIGGQDLNDGNsTLTLALVWQLMRR 572
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 84-150 2.41e-15

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: 70.65  E-value: 2.41e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKEANLPLPgykvREIIQRLMADGDKNKDGKIGFDEFVYIFQ 150
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 590-691 4.06e-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: 68.50  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  590 DIIVRWVNRTLAEAGKSTSiqSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGdLSEDDKHDNAKFAVSMARRIG-ARV 668
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS-LSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 1717014095  669 YALPEDLVEvKPKMVMTVFACLM 691
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
EF-hand_7 pfam13499
EF-hand domain pair;
83-150 2.06e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.57  E-value: 2.06e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717014095  83 EELREAFARVDLDNSGFISDYELHDLFKEANLPLPgyKVREIIQRLMADGDKNKDGKIGFDEFVYIFQ 150
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-156 1.67e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  76 QISKDEL-------------EELREAFARVDLDNSGFISDYELHDLFKEANLPlpgykvREIIQRLMADGDKNKDGKIGF 142
Cdd:COG5126    49 RISREEFvagmeslfeatvePFARAAFDLLDTDGDGKISADEFRRLLTALGVS------EEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|....
gi 1717014095 143 DEFVYIFQELKSSD 156
Cdd:COG5126   123 EEFVAAVRDYYTPD 136
PTZ00183 PTZ00183
centrin; Provisional
 76-148 3.04e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 47.76  E-value: 3.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717014095  76 QISKDELEELREAFARVDLDNSGFISDYElhdlFKEANLPLPGYKVREIIQRLMADGDKNKDGKIGFDEFVYI 148
Cdd:PTZ00183   10 GLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 125-152 3.94e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 38.13  E-value: 3.94e-04
                           10        20
                   ....*....|....*....|....*...
gi 1717014095  125 IQRLMADGDKNKDGKIGFDEFVYIFQEL 152
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 169-313 2.20e-107

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: 321.92  E-value: 2.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIEL 313
Cdd:cd21292    81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 445-578 6.28e-98

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: 297.30  E-value: 6.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 445 YPALTKPVNQDIDWTLLEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 524
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 525 MKKLENCNYAVDLGKYPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
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 ...
 169-316 6.21e-97

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: 295.43  E-value: 6.21e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21325     1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIELSKN 316
Cdd:cd21325    81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 169-313 2.15e-96

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: 293.87  E-value: 2.15e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21323     1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIEL 313
Cdd:cd21323    81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 169-313 5.77e-93

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: 284.98  E-value: 5.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 169 EGICAIGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDE 248
Cdd:cd21324     1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095 249 RVINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIEL 313
Cdd:cd21324    81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 322-443 1.07e-89

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: 275.31  E-value: 1.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 322 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEERIDINMSGFSEKDD 401
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 402 LKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21328    81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
53-691 1.36e-87

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 286.84  E-value: 1.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  53 LEENKLvsQRYYTSQFHKMANTAQISKDEleelrEAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLmadg 132
Cdd:COG5069     1 MEAKKW--QKVQKKTFTKWTNEKLISGGQ-----KEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVM---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 133 dKNKDGKIGFDEFV--YIFQELKSsDIAKTFRKAInrkegicaIGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPD 210
Cdd:COG5069    70 -ENVSGRLEFIKGKgvKLFNIGPQ-DIVDGNPKLI--------LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDED 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 211 CQHVLPmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAE 285
Cdd:COG5069   138 TGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIP 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 286 DLKAgkpHLVLgLLWQIIKIGLFADIELSKNEaLAALLRDGETLEDlMKLSPEELLLRWAN-FHLENAGWNkINNFSSDI 364
Cdd:COG5069   217 DERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK-VVNFSKDV 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 365 KDSRAYFHLLNQIAPKGQKEGEERIDInmsgfsekddLKRAEYMLQQADRLGCRQFVTPAdvvsGNPKLNLAFVANLFNK 444
Cdd:COG5069   290 SDGENYTDLLNQLNALCSRAPLETTDL----------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNT 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 445 YPALtKPVNQ----DIDWTLLEGEtREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVP--VDWNKVNKPPY 518
Cdd:COG5069   356 HPGQ-EPLEEeekpEIEEFDAEGE-FEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPA 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 519 PKLGAN-MKKLENCNYAVDLGKyPAKFSLVGIGGQDLNDGNStLTLALVWQLMRRYSLNVLEDLG-DGQKVNDDIIVRWV 596
Cdd:COG5069   434 SGIEENrFKAFENENYAVDLGI-TEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWL 511

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 597 NRTLAEAGKSTSIQSFKDKTISTSWA-VVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVS--MARRIGARVYALPE 673
Cdd:COG5069   512 GSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPE 591

                         650
                  ....*....|....*....
gi 1717014095 674 DLVEVKPKM-VMTVFACLM 691
Cdd:COG5069   592 DINGVRPRLdVLTFIESLM 610
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 454-578 1.41e-79

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: 249.14  E-value: 1.41e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 454 QDIDWTLLEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGANMKKLENCNY 533
Cdd:cd21330     1 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1717014095 534 AVDLGKYPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21330    81 AVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 322-446 1.36e-78

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: 246.41  E-value: 1.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 322 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEERIDINMSGFSEKDD 401
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1717014095 402 LKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 446
Cdd:cd21327    81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 587-698 4.95e-75

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: 236.71  E-value: 4.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLMGRGMKKV 698
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 461-578 8.30e-74

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: 233.67  E-value: 8.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 461 LEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGANMKKLENCNYAVDLGKY 540
Cdd:cd21298     1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 541 PaKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21298    81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 461-578 1.06e-73

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: 233.34  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 461 LEGETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGANMKKLENCNYAVDLGKY 540
Cdd:cd21329     1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 541 PAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21329    81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 325-446 2.24e-72

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: 230.16  E-value: 2.24e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 325 DGETLEDLMKLSPEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEErIDINMSGFSEKDDLKR 404
Cdd:cd21326     1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFDEN-IEIDFSGFNEKNDLKR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 405 AEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 446
Cdd:cd21326    80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 325-443 2.30e-68

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: 2.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 325 DGETLEDLMKLSPEELLLRWANFHLENAGWNK-INNFSSDIKDSRAYFHLLNQIAPKGQKEGeeridinMSGFSEKDDLK 403
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIKDSEAYTHLLKQIAPKDAGVD-------TSALRESDLLQ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1717014095 404 RAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21295    74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 582-696 1.91e-67

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: 216.78  E-value: 1.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 582 GDGQKVNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVSMA 661
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717014095 662 RRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 696
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 587-694 1.05e-58

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: 193.27  E-value: 1.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKiGDLSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21301     1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVL-EGNSEEDKLSNAKYAISMARKIGA 79

                          90       100
                  ....*....|....*....|....*...
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLMGRG 694
Cdd:cd21301    80 RVYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 580-694 1.41e-58

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: 193.24  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 580 DLGDGQKVNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFAVS 659
Cdd:cd21332     1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717014095 660 MARRIGARVYALPEDLVEVKPKMVMTVFACLMGRG 694
Cdd:cd21332    81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 192-304 3.64e-55

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: 183.93  E-value: 3.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 192 EEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKK-LTPFTIQENLNLALN 270
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 271 SASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21217    81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 463-578 1.09e-51

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: 174.39  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 463 GETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKV-PVDWNKVNKppyPKLGANMKKLENCNYAVDLGKyP 541
Cdd:cd21219     1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNK---PKPLNKFKKVENCNYAVDLAK-K 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 542 AKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21219    77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 193-305 3.13e-46

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: 160.00  E-value: 3.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVIN-KKKLTPFTIQENLNLALNS 271
Cdd:cd21293     2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKI 305
Cdd:cd21293    82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 327-443 8.38e-46

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: 158.62  E-value: 8.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 327 ETLEDLMKLSPEELLLRWANFHLENAGWNK--INNFSSDIKDSRAYFHLLNQIAPKGQKEgeeriDINMSGFSEKDDLKR 404
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDK-----ELVLEVLSEEDLEKR 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1717014095 405 AEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21218    76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 461-578 2.26e-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: 154.89  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 461 LEGEtREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIkVP--VDWNKVNKPPYPKLGANMKKLENCNYAVDLG 538
Cdd:cd21300     3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1717014095 539 KyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21300    81 K-QLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 187-306 7.25e-44

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: 153.76  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 187 HSYSEEEKYAFVNWINKALENDPDCQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINK-----KKLTPFTI 261
Cdd:cd21294     1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1717014095 262 QENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIG 306
Cdd:cd21294    81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 587-691 5.15e-42

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: 147.80  E-value: 5.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGdLSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21220     1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEG-ETDEEKEQNAKYAISLARKIGA 79

                          90       100
                  ....*....|....*....|....*
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLM 691
Cdd:cd21220    80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 327-443 9.27e-38

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: 136.15  E-value: 9.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 327 ETLEDLMKLSPEELLLRWANFHLENAGWN-KINNFSSDIKDSRAYFHLLNQIAPKGQKEGEeridinmsgFSEKDDLKRA 405
Cdd:cd21297     1 ETLEQFLRLPPEQILLRWFNYHLKAANWPrRVSNFSKDVSDGENYTVLLNQLAPELCSRAP---------LQTTDLLQRA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 406 EYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21297    72 EQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 327-442 2.31e-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: 126.48  E-value: 2.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 327 ETLEDLMKLSPEELLLRWANFHLENAGWNK-INNFSSDIKDSRAYFHLLNQIAPKGQkegeeridiNMSGFSEKDDLKRA 405
Cdd:cd21296     1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSDVKDAEAYAYLLNVLAPEHC---------DPATLEAKDPLERA 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 406 EYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLF 442
Cdd:cd21296    72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 463-578 1.18e-33

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: 124.54  E-value: 1.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 463 GETREERTFRNWMNSLGVKPHVNHLYSDLQDALVILQLYEKIKV-PVDWNKVNKPPyPKLgaNMKKLENCNYAVDLGKyP 541
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPgSVNWKHANKPP-IKM--PFKKVENCNQVVKIGK-Q 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 542 AKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVL 578
Cdd:cd21299    77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 584-691 1.38e-30

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: 115.60  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 584 GQKVNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDlSEDDKHDNAKFAVSMARR 663
Cdd:cd21303     1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGN-TEDEAYLNAKLAISIARK 79

                          90       100
                  ....*....|....*....|....*...
gi 1717014095 664 IGARVYALPEDLVEVKPKMVMTVFACLM 691
Cdd:cd21303    80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 587-691 9.97e-25

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


Pssm-ID: 409151  Cd Length: 109  Bit Score: 99.17  E-value: 9.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 587 VNDDIIVRWVNRTLAEAGKSTSIQSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGDlSEDDKHDNAKFAVSMARRIGA 666
Cdd:cd21302     2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGE-TDEEKRLNATYIISVARKLGC 80

                          90       100
                  ....*....|....*....|....*
gi 1717014095 667 RVYALPEDLVEVKPKMVMTVFACLM 691
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 335-447 9.70e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 96.20  E-value: 9.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 335 LSPEELLLRWANFHLENAGWNK-INNFSSDIKDSRAYFHLLNQIAPKGQKEGEERidinmsgFSEKDDLKRAEYMLQQAD 413
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrVTNFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENINLALDVAE 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 414 R-LGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 447
Cdd:pfam00307  74 KkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 191-306 1.67e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 95.82  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 191 EEEKYAFVNWINKALENDPDCQHVlpmnpntNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKkltPFTIQENLNLALN 270
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 271 SAS-AIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIG 306
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 195-305 6.35e-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: 90.84  E-value: 6.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  195 YAFVNWINKALENDPdcqhvlpmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKlTPFTIQENLNLALNSASA 274
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1717014095  275 IGCHVVNIGAEDLKAGkPHLVLGLLWQIIKI 305
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 589-696 4.50e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.10  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 589 DDIIVRWVNRTLAEAGKSTSIQSFKdKTISTSWAVVDLIDAIQPGCINYDLVKIgdlSEDDKHDNAKFAVSMARR-IGAR 667
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK---SEFDKLENINLALDVAEKkLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1717014095 668 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 696
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 467-573 5.75e-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: 80.02  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNSL----GVKPHVNHLYSDLQDALVILQLYEKIKvP--VDWNKVNKPPypklganMKKLENCNYAVDLGKY 540
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 541 PAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 339-444 1.64e-17

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: 78.13  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  339 ELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEgeeriDINMSGFSEKDDLKRAEYMLQQADRLGC- 417
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLALSFAEKLGGk 75

                           90       100
                   ....*....|....*....|....*..
gi 1717014095  418 RQFVTPADVVSGnPKLNLAFVANLFNK 444
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 194-304 1.60e-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: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 194 KYAFVNWINKALENDPdcqhvlpmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDErvINKKKLTPFTIQENLNLALNSAS 273
Cdd:cd00014     1 EEELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACK 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 274 AIG-CHVVNIGAEDLKAGK-PHLVLGLLWQIIK 304
Cdd:cd00014    71 KLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 469-572 4.57e-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: 74.27  E-value: 4.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  469 RTFRNWMNSLGVK---PHVNHLYSDLQDALVILQLYEKIKVP-VDWNKVNKPPYPklganMKKLENCNYAVDLGKyPAKF 544
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74

                           90       100
                   ....*....|....*....|....*...
gi 1717014095  545 SLVGIGGQDLNDGNsTLTLALVWQLMRR 572
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 84-150 2.41e-15

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: 70.65  E-value: 2.41e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKEANLPLPgykvREIIQRLMADGDKNKDGKIGFDEFVYIFQ 150
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 190-304 5.51e-15

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 71.54  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 190 SEEEKyAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTID-ERVINKKKLTPFTIQENLNLA 268
Cdd:cd21219     3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNwKKVNKPKPLNKFKKVENCNYA 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 269 LNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21219    71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 590-691 4.06e-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: 68.50  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  590 DIIVRWVNRTLAEAGKSTSiqSFKDKTISTSWAVVDLIDAIQPGCINYDLVKIGdLSEDDKHDNAKFAVSMARRIG-ARV 668
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS-LSRFKKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 1717014095  669 YALPEDLVEvKPKMVMTVFACLM 691
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 467-572 6.50e-13

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: 65.78  E-value: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNSLGVKP--HVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVDLGKypAKF 544
Cdd:cd21193    17 QKKTFTKWINSFLEKAnlEIGDLFTDLSDGKLLLKLLEIIS----GEKLGKPNRGRL--RVQKIENVNKALAFLK--TKV 88

                          90       100
                  ....*....|....*....|....*...
gi 1717014095 545 SLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21193    89 RLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 467-573 8.17e-12

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: 62.42  E-value: 8.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMN----SLGVKphVNHLYSDLQDALVILQLYEKIkvpvdwNKVNKPPY---PKLgaNMKKLENCNYAVDLGK 539
Cdd:cd21215     5 QKKTFTKWLNtklsSRGLS--ITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIK 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 540 yPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:cd21215    75 -SRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
EF-hand_7 pfam13499
EF-hand domain pair;
83-150 2.06e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.57  E-value: 2.06e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717014095  83 EELREAFARVDLDNSGFISDYELHDLFKEANLPLPgyKVREIIQRLMADGDKNKDGKIGFDEFVYIFQ 150
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 190-304 5.88e-11

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: 59.94  E-value: 5.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 190 SEEEKyAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINK---KKLTPFTIQENLN 266
Cdd:cd21298     5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 267 LALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21298    73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 191-303 6.26e-11

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 59.61  E-value: 6.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 191 EEEKYAFVNWINKALEndpdcqhvlPMNPNTNDLFKAVGDGIVLCKMInlsvpDTIDERVI---NKKKLTPFTIQENLNL 267
Cdd:cd21227     3 EIQKNTFTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALV-----EILQGRKLgrvIKKPLNQHQKLENVTL 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 268 ALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21227    69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 462-572 1.21e-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: 60.04  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKVpvdwnkvNKPPYPKLG-ANMKKLENCNYAVDLG 538
Cdd:cd21318    34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-------EQLPKPTRGrMRIHSLENVDKALQFL 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 539 KyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21318   107 K-EQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 462-572 1.70e-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: 58.92  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLGANMkkLENCNYAVDLGK 539
Cdd:cd21246    12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGKMRIHC--LENVDKALQFLK 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 540 yPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21246    86 -EQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 462-576 7.24e-10

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: 57.30  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKVpvdwnkvNKPPYPKLGANMKKLENCNYAVDLGK 539
Cdd:cd21236    13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSG-------DTLPREKGRMRFHRLQNVQIALDYLK 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 540 yPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLN 576
Cdd:cd21236    86 -RRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 183-303 1.03e-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: 56.38  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 183 EGTQhsyseeeKYAFVNWINKALEndpdcQHVLPmnPNTNDLFKAVGDGIVLCKMIN-LSvpdtiDERVINKKKLTPFTI 261
Cdd:cd21242     3 EQTQ-------KRTFTNWINSQLA-----KHSPP--SVVSDLFTDIQDGHRLLDLLEvLS-----GQQLPREKGHNVFQC 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 262 QENLNLALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21242    64 RSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 193-303 1.34e-09

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 56.15  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALEndpdcqhvlPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDErvINKKKLTPFTIqENLNLALNSA 272
Cdd:cd21193    17 QKKTFTKWINSFLE---------KANLEIGDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAiGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21193    85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-156 1.67e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  76 QISKDEL-------------EELREAFARVDLDNSGFISDYELHDLFKEANLPlpgykvREIIQRLMADGDKNKDGKIGF 142
Cdd:COG5126    49 RISREEFvagmeslfeatvePFARAAFDLLDTDGDGKISADEFRRLLTALGVS------EEEADELFARLDTDGDGKISF 122

                          90
                  ....*....|....
gi 1717014095 143 DEFVYIFQELKSSD 156
Cdd:COG5126   123 EEFVAAVRDYYTPD 136
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 191-307 2.55e-09

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 55.51  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 191 EEEKYAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKK----LTPFTIQENLN 266
Cdd:cd21300     6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1717014095 267 LALNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGL 307
Cdd:cd21300    75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHI 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 193-312 3.00e-09

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 55.07  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALendpdCQHVLPMNpnTNDLFKAVGDGIVLCKMIN-LSVPDTIDERVINKKKLTPFTiqeNLNLALNS 271
Cdd:cd21241     6 QKKTFTNWINSYL-----AKRKPPMK--VEDLFEDIKDGTKLLALLEvLSGEKLPCEKGRRLKRVHFLS---NINTALKF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIkigLFADIE 312
Cdd:cd21241    76 LESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 193-304 6.09e-09

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: 53.94  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALENdpdcqhvlpMNPNTNDLFKAVGDGIVLCKMINLsVPDTIDERVINKKKLTpftIQ--ENLNLALN 270
Cdd:cd21215     5 QKKTFTKWLNTKLSS---------RGLSITDLVTDLSDGVRLIQLLEI-IGDESLGRYNKNPKMR---VQklENVNKALE 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 271 SASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21215    72 FIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 467-571 7.67e-09

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 54.12  E-value: 7.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNS-LGVKPHVNH----------LYSDLQDALVILQLYEKIKvP--VDWNKVNKPPyPKlgANMKKLENCNY 533
Cdd:cd21217     2 EKEAFVEHINSlLADDPDLKHllpidpdgddLFEALRDGVLLCKLINKIV-PgtIDERKLNKKK-PK--NIFEATENLNL 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 534 AVDLGKyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMR 571
Cdd:cd21217    78 ALNAAK-KIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 462-576 1.19e-08

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: 53.50  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS--LGVKPHVNHLYSDLQDA---LVILQLYEKIKVPVDWNKVNkppypklganMKKLENCNYAVD 536
Cdd:cd21237     2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSGVKLPREKGRMR----------FHRLQNVQIALD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1717014095 537 LGKyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLN 576
Cdd:cd21237    72 FLK-QRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 462-572 1.21e-08

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 53.90  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS-LG-VKPHVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVDLGK 539
Cdd:cd21317    27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLS----GEQLPKPTKGRM--RIHCLENVDKALQFLK 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 540 yPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21317   101 -EQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 193-303 1.87e-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: 53.45  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDErvinKKKLTPFTIQENLNLALNSA 272
Cdd:cd21236    18 QKKTFTKWIN---------QHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21236    85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 336-431 2.68e-08

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: 52.24  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 336 SPEELLLRWANFHLENAgwnKINNFSSDIKDSRAYFHLLNQIAPkGQkegeerIDINMSgFSEKDDLKRAEYMLQQA-DR 414
Cdd:cd21184     1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKP-GL------IPDNES-LDKENPLENATKAMDIAeEE 69

                          90
                  ....*....|....*..
gi 1717014095 415 LGCRQFVTPADVVSGNP 431
Cdd:cd21184    70 LGIPKIITPEDMVSPNV 86
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 467-567 3.25e-08

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: 52.00  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNSLGVK---PHVNHLYSDLQDALVILQLYEKIKvpvdwnkvnkppypklGANMKK---------LENCNYA 534
Cdd:cd21186     3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVLT----------------GKKLKPekgrmrvhhLNNVNRA 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 535 VD-LGKYPAKfsLVGIGGQDLNDGNSTLTLALVW 567
Cdd:cd21186    67 LQvLEQNNVK--LVNISSNDIVDGNPKLTLGLVW 98
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 462-570 3.39e-08

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: 52.23  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNSLGVK---PHVNHLYSDLQDALVILQLYEKIKVpvdwnkvNKPPYPKLGANMKKLENCNYAVDLG 538
Cdd:cd21231     2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-------QKLVKEKGSTRVHALNNVNKALQVL 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 539 KyPAKFSLVGIGGQDLNDGNSTLTLALVWQLM 570
Cdd:cd21231    75 Q-KNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 462-582 3.82e-08

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: 52.33  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNSLGVKP--HVNHLYSDLQDALVILQLYEKIKVpvdwnkvNKPPYPKLGANMKKLENCNYAVDLGK 539
Cdd:cd21235     2 ERDRVQKKTFTKWVNKHLIKAqrHISDLYEDLRDGHNLISLLEVLSG-------DSLPREKGRMRFHKLQNVQIALDYLR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1717014095 540 YpAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNVLEDLG 582
Cdd:cd21235    75 H-RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSG 116
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 467-567 5.32e-08

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 51.25  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVDLGKYpA 542
Cdd:cd21188     4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL---------SGESLPRERGRMRfhRLQNVQTALDFLKY-R 73

                          90       100
                  ....*....|....*....|....*
gi 1717014095 543 KFSLVGIGGQDLNDGNSTLTLALVW 567
Cdd:cd21188    74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 467-573 6.79e-08

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: 51.13  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNsLGVKPH---VNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPklganMKKLENCNYAVDLGKYPAk 543
Cdd:cd21227     5 QKNTFTNWVN-EQLKPTgmsVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQ-----HQKLENVTLALKAMAEDG- 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1717014095 544 FSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:cd21227    78 IKLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 193-303 7.55e-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: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcqHVLPMNPNTNDLFKAVGDGIVLCKMI-NLSvpdtiDERVINKKKLTPFTIQENLNLALNS 271
Cdd:cd21188     4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLeVLS-----GESLPRERGRMRFHRLQNVQTALDF 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21188    70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 338-442 1.16e-07

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: 50.35  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 338 EELLLRWANFHLENAG-WNKINNFSS-DIKDSRAYFHLLNQIAPkgqkeGEERIDINMSGFSEKDDLKRAEYMLQQADRL 415
Cdd:cd21220     3 DADILAWANSKVREAGkSSPISSFKDpSLSTGLFLLDLLAAIDP-----GAVDYDLVTEGETDEEKEQNAKYAISLARKI 77

                          90       100
                  ....*....|....*....|....*..
gi 1717014095 416 GCRQFVTPADVVSGNPKLNLAFVANLF 442
Cdd:cd21220    78 GAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 341-441 1.34e-07

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: 50.36  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 341 LLRWANFHLENAG-WNKINNFS-SDIKDSRAYFHLLNQIAPKGqkegeerIDINM--SGFSEKDDLKRAEYMLQQADRLG 416
Cdd:cd21301     6 IVEWANEKLKSAGkSTSISSFKdPSISTSLPILDLIDAIKPGS-------VDYSLvlEGNSEEDKLSNAKYAISMARKIG 78

                          90       100
                  ....*....|....*....|....*
gi 1717014095 417 CRQFVTPADVVSGNPKLNLAFVANL 441
Cdd:cd21301    79 ARVYALPEDIVEVKPKMVMTVFACL 103
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 193-303 1.35e-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: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLsVPDTIDERVINKKKLTPFTIQENLNLALNSA 272
Cdd:cd21183     5 QANTFTRWCN---------EHLKERGMQIHDLATDFSDGLCLIALLEN-LSTRPLKRSYNRRPAFQQHYLENVSTALKFI 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21183    75 EADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 193-312 1.75e-07

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: 50.26  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALEndpdcQHVLPMNpnTNDLFKAVGDGIVLCKMINLSVPDTIDERviNKKKLTPFTIQENLNLALNSA 272
Cdd:cd21190     6 QKKTFTNWINSHLA-----KLSQPIV--INDLFVDIKDGTALLRLLEVLSGQKLPIE--SGRVLQRAHKLSNIRNALDFL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIkigLFADIE 312
Cdd:cd21190    77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 80-163 1.93e-07

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 51.38  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  80 DELEELREAFARVDLDNSGFISDYELHDLFKEAnlplpGYKV-REIIQRLMADGDKNKDGKIGFDEFVYIFQELKSsdIA 158
Cdd:cd16180    64 KYIQDWRRLFRRFDRDRSGSIDFNELQNALSSF-----GYRLsPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKR--LT 136


                  ....*
gi 1717014095 159 KTFRK 163
Cdd:cd16180   137 DAFRK 141
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 465-575 2.00e-07

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: 50.14  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 465 TREERTFRNWMNSL----GVKPHVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLGANMkkLENCNYAVDLGKY 540
Cdd:cd21247    19 TMQKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELIS----GEQLPRPSRGKMRVHF--LENNSKAITFLKT 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717014095 541 PAKFSLvgIGGQDLNDGNSTLTLALVWQLMRRYSL 575
Cdd:cd21247    93 KVPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 464-574 3.56e-07

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: 49.07  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 464 ETREERTFRNWMNSLGVK---PHVNHLYSDLQDALVILQLYEKIKvpvdwNKVNKPPYPKLGAN-MKKLENCNYAVDLGK 539
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKrgiPKISDLATDLSDGVRLIFFLELVS-----GKKFPKKFDLEPKNrIQMIQNLHLAMLFIE 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717014095 540 YPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYS 574
Cdd:cd21225    77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 467-570 3.67e-07

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: 48.85  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMN---SLGVKPHVNHLYSDLQDALVILQLYEKIkvpvdwnkVNKP-PYPKLGANMKKLENCNYAVDLgKYPA 542
Cdd:cd21232     3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGL--------TGKSlPKERGSTRVHALNNVNRVLQV-LHQN 73

                          90       100
                  ....*....|....*....|....*...
gi 1717014095 543 KFSLVGIGGQDLNDGNSTLTLALVWQLM 570
Cdd:cd21232    74 NVELVNIGGTDIVDGNHKLTLGLLWSII 101
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 83-146 5.19e-07

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 51.59  E-value: 5.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717014095  83 EELREAFARVDLDNSGFISDYEL----HDLFKEANLPLPGYKVREIIQRLMADGDKNKDGKIGFDEFV 146
Cdd:cd15902    90 VEFMKIWRKYDTDGSGFIEAKELkgflKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMA 157
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 323-444 6.74e-07

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: 48.41  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 323 LRDGETLEDlmklspeELLLRWANFHLENAgwNKINNFSS----DIKDSRAYFHLLNQIAPKG-QKEGEERIDinmsgFS 397
Cdd:cd21332     2 LGEGEKVND-------EIIIKWVNQTLANA--NKTTSITSfkdkSISTSLPVLDLIDAIAPNAiREEMVKRED-----LS 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1717014095 398 EKDDLKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFNK 444
Cdd:cd21332    68 DADKLNNAKYAISVARKIGARVYALPEDLVEVKPKMVMTVFACLMGK 114
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 190-304 8.80e-07

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 48.27  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 190 SEEEKyAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKLT-PFTIQENLNLA 268
Cdd:cd21299     3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 269 LNSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21299    71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 193-303 9.76e-07

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: 48.13  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMIN-LSvpdtiDERV--INKKKLTPFTIqENLNLAL 269
Cdd:cd21246    17 QKKTFTKWVN---------SHLARVGCRINDLYTDLRDGRMLIKLLEvLS-----GERLpkPTKGKMRIHCL-ENVDKAL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 270 NSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21246    82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 464-570 1.00e-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: 47.77  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 464 ETREERTFRNWMNS----LGVKphVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVD-LG 538
Cdd:cd21214     3 EKQQRKTFTAWCNShlrkAGTQ--IENIEEDFRDGLKLMLLLEVIS----GERLPKPERGKM--RFHKIANVNKALDfIA 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 539 KYPAKfsLVGIGGQDLNDGNSTLTLALVWQLM 570
Cdd:cd21214    75 SKGVK--LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 446-577 1.45e-06

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: 47.72  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 446 PALTKPVNQDIDWTLLEgetreERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLGA 523
Cdd:cd21310     1 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLS----QKKMYRKYHPRPNF 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 524 NMKKLENCNYAVDLGKYpAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNV 577
Cdd:cd21310    72 RQMKLENVSVALEFLDR-EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 64-151 1.48e-06

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


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 47.14  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  64 YTSQFHKMAntaqISKDELEELREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIiQRLMADGDKNKDGKIGFD 143
Cdd:cd16251    19 YKKFFEHVG----LKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRDLTDEET-KALLAAGDTDGDGKIGVE 93


                  ....*...
gi 1717014095 144 EFVYIFQE 151
Cdd:cd16251    94 EFATLVAG 101
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 338-444 1.50e-06

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: 47.58  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 338 EELLLRWANFHLENAGWN-KINNF-SSDIKDSRAYFHLLNQIAPkgqkeGEERIDINMSG-FSEKDDLKRAEYMLQQADR 414
Cdd:cd21334     3 DDIIVNWVNRTLSEAGKStSIQNFkDKTISSSLAVVDLIDAIQP-----GCINYDLVKTGnLTDDDKLDNAKYAVSMARK 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1717014095 415 LGCRQFVTPADVVSGNPKLNLAFVANLFNK 444
Cdd:cd21334    78 IGARVYALPEDLVEVKPKMVMTVFACLMGR 107
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 77-151 2.42e-06

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


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 46.35  E-value: 2.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717014095  77 ISKDELEELREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIiQRLMADGDKNKDGKIGFDEFVYIFQE 151
Cdd:cd16254    28 LKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSDKET-KALLAAGDKDGDGKIGIDEFATLVAE 101
PTZ00183 PTZ00183
centrin; Provisional
 76-148 3.04e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 47.76  E-value: 3.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717014095  76 QISKDELEELREAFARVDLDNSGFISDYElhdlFKEANLPLPGYKVREIIQRLMADGDKNKDGKIGFDEFVYI 148
Cdd:PTZ00183   10 GLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 462-573 3.38e-06

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: 46.21  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNSLGVK--P--HVNHLYSDLQDALVILQLYEKIkvpvdwnKVNKPPYPKlGANMKK---LENCNYA 534
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKrkPpmKVEDLFEDIKDGTKLLALLEVL-------SGEKLPCEK-GRRLKRvhfLSNINTA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1717014095 535 VDL--GKypaKFSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:cd21241    73 LKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 85-164 3.40e-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: 47.22  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  85 LREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLmadgDKNKDGKIGFDEFVYIFQEL-KSSDIAKTFRK 163
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEA----DTSGEDVLDEEEFVQFYNRLtKRPEIEELFKK 77


                  .
gi 1717014095 164 A 164
Cdd:cd16202    78 Y 78
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 462-572 3.41e-06

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: 47.35  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVDLGK 539
Cdd:cd21316    49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 122

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 540 yPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21316   123 -EQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 193-314 3.46e-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: 46.56  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcqHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDErvinKKKLTPFTIQENLNLALNSA 272
Cdd:cd21235     7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIELS 314
Cdd:cd21235    74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 190-304 3.75e-06

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 46.52  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 190 SEEEKyAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLS-VPdtIDERVINKKkltPFTIQ------ 262
Cdd:cd21329     5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTrVP--VDWGHVNKP---PYPALggnmkk 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1717014095 263 -ENLNLALN-SASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21329    68 iENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 467-573 4.34e-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: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKI---KVPVDWNKvnKPPYPKlganmKKLENCNYAVDLGKyP 541
Cdd:cd21183     5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLstrPLKRSYNR--RPAFQQ-----HYLENVSTALKFIE-A 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 542 AKFSLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:cd21183    77 DHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 462-575 7.12e-06

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: 45.65  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMN----SLGVKPHVNHLYSDLQDALVILQLYEKIKvpvDWNKVNKppYPKLGANMKKLENCNYAVDL 537
Cdd:cd21191     1 ERENVQKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLS---GQNLLQE--YKPSSHRIFRLNNIAKALKF 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1717014095 538 GKyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSL 575
Cdd:cd21191    76 LE-DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 193-304 7.20e-06

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 46.15  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMIN-LSVPdtIDERVINK----------KKLtpfti 261
Cdd:cd21331    23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKppypklganmKKL----- 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1717014095 262 qENLNLALN-SASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21331    85 -ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 85-165 7.98e-06

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 46.12  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  85 LREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLmadgDKNKDGKIGFDEFVYIFQELkssdiakTFRKA 164
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEV----DTNGDGTLTFDEFEELYKSL-------TERPE 70


                  .
gi 1717014095 165 I 165
Cdd:cd15898    71 L 71
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 454-575 8.34e-06

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 45.52  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 454 QDIDWTLLEgetreERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKI---KVPvdwnKVNKPPypklgaNMK-- 526
Cdd:cd21311     8 EDAQWKRIQ-----QNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsq 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1717014095 527 KLENCNYAVDLGKYPAKFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSL 575
Cdd:cd21311    73 KLENVSVALKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 446-577 8.52e-06

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: 45.85  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 446 PALTKPVNQDIDWTLLEgetreERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKlga 523
Cdd:cd21308     5 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR--- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 524 nMKKLENCNYAVDLGKYPAkFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNV 577
Cdd:cd21308    77 -QMQLENVSVALEFLDRES-IKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 193-314 9.76e-06

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: 45.41  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcqHVLPMNPNTNDLFKAVGDGIVLCKMinLSVPDTIdeRVINKKKLTPFTIQENLNLALNSA 272
Cdd:cd21237     7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISL--LEVLSGV--KLPREKGRMRFHRLQNVQIALDFL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIKIGLFADIELS 314
Cdd:cd21237    74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 84-170 1.11e-05

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: 46.05  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKEANLPLpGYKVreiIQRLMADGDKNKDGKIGFDEFVYIFQELksSDIAKTFRK 163
Cdd:cd16185     1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLF-SLAT---AEKLIRMFDRDGNGTIDFEEFAALHQFL--SNMQNGFEQ 74


                  ....*..
gi 1717014095 164 AINRKEG 170
Cdd:cd16185    75 RDTSRSG 81
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 446-577 1.18e-05

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: 45.46  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 446 PALTKPVNQDIDWTLLEgetreERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKlga 523
Cdd:cd21309     2 PVTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFR--- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717014095 524 nMKKLENCNYAVDLGKYPAkFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSLNV 577
Cdd:cd21309    74 -QMQLENVSVALEFLDRES-IKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 193-303 1.21e-05

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: 45.40  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKLTPFtiqENLNLALNSA 272
Cdd:cd21318    39 QKKTFTKWVN---------SHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21318   107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 589-684 1.38e-05

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: 44.60  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 589 DDIIVRWVNRTLAEAG-KSTSIQSF----KDktiSTSWAVvdLIDAIQPGCINYDLVKIgDLSEDDKHDNAKFAVSMARR 663
Cdd:cd21218    12 EEILLRWVNYHLKKAGpTKKRVTNFssdlKD---GEVYAL--LLHSLAPELCDKELVLE-VLSEEDLEKRAEKVLQAAEK 85

                          90       100
                  ....*....|....*....|.
gi 1717014095 664 IGARVYALPEDLVEVKPKMVM 684
Cdd:cd21218    86 LGCKYFLTPEDIVSGNPRLNL 106
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 579-690 1.39e-05

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 44.87  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 579 EDLGDGQKVN-DDIIVRWVNRTLAEAGKSTsIQSFKdKTISTSWAVVDLIDAIQPGCINYDLVKIGDLSEDDKHDNAKFA 657
Cdd:cd21326     3 EELEELMKLSpEELLLRWVNYHLTNAGWQN-ISNFS-QDIKDSRAYFHLLNQIAPKGDVFDENIEIDFSGFNEKNDLKRA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 658 VSM---ARRIGARVYALPEDLVEVKPKMVMTVFACL 690
Cdd:cd21326    81 EYMlqeADKLGCRQFVTPADVVSGNPKLNLAFVANL 116
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 579-690 2.14e-05

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: 44.19  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 579 EDLGDGQKVN-DDIIVRWVNRTLAEAGKSTSIQSFKdKTISTSWAVVDLIDAIQPGCinyDLVKIGDLSEDDKHDNAKFA 657
Cdd:cd21295     3 ETLEDLLKLSpEEILLRWVNYHLERAGCDRRIKNFS-GDIKDSEAYTHLLKQIAPKD---AGVDTSALRESDLLQRAELM 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1717014095 658 VSMARRIGARVYALPEDLVEVKPKMVMTVFACL 690
Cdd:cd21295    79 LQNADKIGCRKFVTPKDVVTGNPKLNLAFVANL 111
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 68-146 2.30e-05

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


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 43.57  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  68 FHKMANTAQISKDELEELREAFARVDLDNSGFISDYELHdLFkeanLPLPGYKVREI----IQRLMADGDKNKDGKIGFD 143
Cdd:cd16255    19 FKKFFATSGLSKKSADDVKKVFEIIDQDKSGFIEEEELK-LF----LQNFSSGARELtdaeTKAFLKAGDSDGDGKIGVE 93


                  ...
gi 1717014095 144 EFV 146
Cdd:cd16255    94 EFQ 96
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 84-154 2.48e-05

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 45.21  E-value: 2.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVreiIQRLMADGDKNKDGKIGFDEFVYIFQELKS 154
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIET---VRLMINMFDRDRSGTINFDEFVGLWKYIQD 68
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 325-446 2.72e-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: 44.00  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 325 DGETLEDLMKLSPEELLLRWANFHLENagwNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEEridinmsgFSEKDDLKR 404
Cdd:cd21315     5 EDDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCPDWED--------WDPKDAVKN 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1717014095 405 AEYMLQQADR-LGCRQFVTPADVVsgNPKLNLAFVANLFNKYP 446
Cdd:cd21315    74 AKEAMDLAEDwLDVPQLIKPEEMV--NPKVDELSMMTYLSQFP 114
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 81-146 2.73e-05

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


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 44.91  E-value: 2.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  81 ELEELREAFARVDLDNSGFISDYELHDLFKEAnlplpGYKV-REIIQRLM---ADgdknKDGKIGFDEFV 146
Cdd:cd16182    70 DLKKWQAIFKKFDTDRSGTLSSYELRKALESA-----GFHLsNKVLQALVlryAD----STGRITFEDFV 130
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 65-145 2.92e-05

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


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 43.32  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  65 TSQFHKMA--NTAQISKDELEELREAFARVDLDNSGFISDYELHDLFKEANlplPGYKV---REIiQRLMADGDKNKDGK 139
Cdd:cd16253    14 ADSFDHKAffKAVGLSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFS---DGARVlsdKET-KNFLAAGDSDGDGK 89


                  ....*.
gi 1717014095 140 IGFDEF 145
Cdd:cd16253    90 IGVDEF 95
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 487-572 3.63e-05

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 43.59  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 487 LYSDLQDALVILQLYEKIkVP--VDWNKVNKPPYPKLGAN-MKKLENCNYAVDLGKyPAKFSLVGIGGQDLNDGNSTLTL 563
Cdd:cd21294    38 LFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKNKPLNnFQMIENNNIVINSAK-AIGCSVVNIGAGDIIEGREHLIL 115


                  ....*....
gi 1717014095 564 ALVWQLMRR 572
Cdd:cd21294   116 GLIWQIIRR 124
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 193-303 3.67e-05

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: 43.14  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALeNDPDCQHVlpmnpntNDLFKAVGDGIVLckminLSVPDTIDERVINKKK-LTPFTIQENLNLALNS 271
Cdd:cd21186     3 QKKTFTKWINSQL-SKANKPPI-------KDLFEDLRDGTRL-----LALLEVLTGKKLKPEKgRMRVHHLNNVNRALQV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21186    70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 87-164 3.86e-05

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 45.81  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  87 EAFARVDLDNSGFISDYELHDLFKEANLPLPGY-----KVREIIQRLMADGDKNKDGKIGFDEFVYIF------------ 149
Cdd:cd15902     3 EVWMHFDADGNGYIEGKELDSFLRELLKALNGKdktddEVAEKKKEFMEKYDENEDGKIEIRELANILpteenflllfrr 82

                          90
                  ....*....|....*..
gi 1717014095 150 --QELKSSDIAKTFRKA 164
Cdd:cd15902    83 eqPLISSVEFMKIWRKY 99
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 192-303 4.08e-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: 43.15  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 192 EEKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLsvpdTIDERVI--NKKKLTPFTIQeNLNLAL 269
Cdd:cd21214     5 QQRKTFTAWCN---------SHLRKAGTQIENIEEDFRDGLKLMLLLEV----ISGERLPkpERGKMRFHKIA-NVNKAL 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 270 NSASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21214    71 DFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 338-443 4.24e-05

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: 43.10  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 338 EELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEgeeridINMSGFSEKDDLKRAEYMLQQADRLGC 417
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK------INKKPKSPFKKRENINLFLNACKKLGL 74

                          90       100
                  ....*....|....*....|....*....
gi 1717014095 418 --RQFVTPADVVS-GNPKLNLAFVANLFN 443
Cdd:cd00014    75 peLDLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 325-444 6.29e-05

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: 43.06  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 325 DGETLEDlmklspeELLLRWANFHLENAGWNK-INNFS-SDIKDSRAYFHLLNQIAPkgqkeGEERID-INMSGFSEKDD 401
Cdd:cd21333     2 GGQKVND-------ETIVNWVNETLTEAGKSSsISSFKdGKISTSMPVLDLIDAIQP-----GSINYDlLKTEDLNDEEK 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1717014095 402 LKRAEYMLQQADRLGCRQFVTPADVVSGNPKLNLAFVANLFNK 444
Cdd:cd21333    70 LNNAKYAISMARKIGARVYALPEDLVEVKPKMVMTVFACLMGR 112
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 462-570 6.77e-05

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 42.56  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNSLGVKPH----VNHLYSDLQDALVILQLYEKI---KVPVDWNKVNKppypklgaNMKKLENCNYA 534
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSqpivINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1717014095 535 VDLGKyPAKFSLVGIGGQDLNDGNSTLTLALVWQLM 570
Cdd:cd21190    73 LDFLT-KRCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 193-303 8.68e-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: 42.57  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALENdpdCQHVLPMNpntnDLFKAVGDGIVLCKMIN-LSVPDTIDERVINKKKLtpFTIQeNLNLALNS 271
Cdd:cd21191     6 QKRTFTRWINLHLEK---CNPPLEVK----DLFVDIQDGKILMALLEvLSGQNLLQEYKPSSHRI--FRLN-NIAKALKF 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21191    76 LEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 336-432 9.50e-05

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 41.98  E-value: 9.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 336 SPEELLLRWANFHLENAgwnKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEEridinmsgFSEKDDLKRAEYMLQQADR- 414
Cdd:cd21230     1 TPKQRLLGWIQNKIPQL---PITNFTTDWNDGRALGALVDSCAPGLCPDWET--------WDPNDALENATEAMQLAEDw 69

                          90
                  ....*....|....*...
gi 1717014095 415 LGCRQFVTPADVVsgNPK 432
Cdd:cd21230    70 LGVPQLITPEEII--NPN 85
PTZ00184 PTZ00184
calmodulin; Provisional
 70-146 9.55e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.21  E-value: 9.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  70 KMANTaqiskDELEELREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLMADGdknkDGKIGFDEFV 146
Cdd:PTZ00184   76 KMKDT-----DSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDG----DGQINYEEFV 143
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 68-152 1.07e-04

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 41.32  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  68 FHKMA----NTAQISKDELEELREAfarvdldnsgfisdyELHDLFKEANLPlpgykvrEIIQRLMADGDKNKDGKIGFD 143
Cdd:cd00213    14 FHKYSgkegDKDTLSKKELKELLET---------------ELPNFLKNQKDP-------EAVDKIMKDLDVNKDGKVDFQ 71


                  ....*....
gi 1717014095 144 EFVYIFQEL 152
Cdd:cd00213    72 EFLVLIGKL 80
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 193-304 1.61e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 41.90  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcqhvLPMNPNTNDLFKAVGDGIVLCKMI-NLSVPdtIDERVINK----------KKLtpfti 261
Cdd:cd21330    14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1717014095 262 qENLNLALN-SASAIGCHVVNIGAEDLKAGKPHLVLGLLWQIIK 304
Cdd:cd21330    76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 83-164 1.75e-04

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 43.67  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  83 EELREAFARVDLDNSGFISDYEL----HDLFKEANLPLPGYKVREIIQRLMADGDKNKDGKIGFDE----------FVYI 148
Cdd:cd16176    85 EEFMQTWRKYDADHSGFIEADELksflKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEmarllpvqenFLLK 164

                          90
                  ....*....|....*.
gi 1717014095 149 FQELKSSdiAKTFRKA 164
Cdd:cd16176   165 FQGVKMC--GKEFNKI 178
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 467-573 2.00e-04

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: 41.32  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNS--LGVKPHVNHLYSDLQDALVILQLYEKIKVPVDWNKVNKPPYPKlganMKKLENCNYAVDLGKyPAKF 544
Cdd:cd21228     5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFR----QMKLENVSVALEFLE-RESI 79

                          90       100
                  ....*....|....*....|....*....
gi 1717014095 545 SLVGIGGQDLNDGNSTLTLALVWQLMRRY 573
Cdd:cd21228    80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 193-302 2.09e-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: 41.03  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALENDPDcqhvlpmNPNTNDLFKAVGDGIVLCKMINLSVPDTIDErvINKKKLTPFTIQENLNLALNSA 272
Cdd:cd21212     1 EIEIYTDWANHYLEKGGH-------KRIITDLQKDLGDGLTLVNLIEAVAGEKVPG--IHSRPKTRAQKLENIQACLQFL 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQI 302
Cdd:cd21212    72 AALGVDVQGITAEDIVDGNLKAILGLFFSL 101
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 85-150 2.20e-04

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 41.93  E-value: 2.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717014095  85 LREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRlmADGDKNKdGKIGFDEFVYIFQ 150
Cdd:cd16220     2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQE--ADTDENQ-GTLTFEEFCVFYK 64
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 87-146 2.23e-04

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 39.90  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  87 EAFARVDLDNSGFISDYELHDLFKEANLPlpgykvREIIQRLMADGDKNKDGKIGFDEFV 146
Cdd:cd00052     3 QIFRSLDPDGDGLISGDEARPFLGKSGLP------RSVLAQIWDLADTDKDGKLDKEEFA 56
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 193-303 3.21e-04

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 40.68  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINlsvpDTIDERVINKKKLTPFTIQENLNLALNSA 272
Cdd:cd21231     7 QKKTFTKWINA--------QFAKFGKPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21231    75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 462-575 3.23e-04

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 40.58  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 462 EGETREERTFRNWMNSLGVKpH-----VNHLYSDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVD 536
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAK-HsppsvVSDLFTDIQDGHRLLDLLEVL-------SGQQLPREKGHNVFQCRSNIETALS 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1717014095 537 LGKYPAkFSLVGIGGQDLNDGNSTLTLALVWQLMRRYSL 575
Cdd:cd21242    73 FLKNKS-IKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 341-443 3.86e-04

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: 40.61  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 341 LLRWANFHLENAGW-NKINNFSSDIKDSRAYF-HLLNQIAPKgqkegeeRIDINMSGFSEKDDLKR--AEYMLQQADRLG 416
Cdd:cd21302     7 ILSWANRKVRTMGRkSQIESFKDKSLSSGLFFlELLWAVEPR-------VVNWNLVTKGETDEEKRlnATYIISVARKLG 79

                          90       100
                  ....*....|....*....|....*..
gi 1717014095 417 CRQFVTPADVVSGNPKLNLAFVANLFN 443
Cdd:cd21302    80 CSIFLLPEDIVEVNQKMILILTASIMY 106
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 125-152 3.94e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 38.13  E-value: 3.94e-04
                           10        20
                   ....*....|....*....|....*...
gi 1717014095  125 IQRLMADGDKNKDGKIGFDEFVYIFQEL 152
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 73-162 4.68e-04

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


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 41.48  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  73 NTAQISKDELEEL-------REAFARVDLDNSGFISDYELHDLFKEAnlplpGYKVR-EIIQRLMADGDKNKDGKIGFDE 144
Cdd:cd16184    50 KSGTIDIYEFQALwnyiqqwKQVFQQFDRDRSGSIDENELHQALSQM-----GYRLSpQFVQFLVSKYDPRARRSLTLDQ 124

                          90
                  ....*....|....*...
gi 1717014095 145 FVYIFQELKSsdIAKTFR 162
Cdd:cd16184   125 FIQVCVQLQS--LTDAFR 140
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 85-169 5.08e-04

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 40.83  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  85 LREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRlmADGDkNKDGKIGFDEFVYIFQELKS-SDIAKTFRK 163
Cdd:cd16205     2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKE--ADTD-DNQGTLDFEEFCAFYKMMSTrRELYLLLLS 78


                  ....*.
gi 1717014095 164 AINRKE 169
Cdd:cd16205    79 YSNKKD 84
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 81-146 5.20e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 42.30  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  81 ELEELREAFARVDLDNSGFISDYELHDLFKEANLP-LPGYkvreIIQRLMADGDKNKDGKIGFDEFV 146
Cdd:cd16227   120 LLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPhMHPV----LIEQTLRDKDKDNDGFISFQEFL 182
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 78-169 5.28e-04

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 42.57  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  78 SKDELEELreaFARVDLDNSGFISDYELHDLFKEANLPLpgykVREIIQRLMADGDKNKDGKIGFDEF---VYIFQELKS 154
Cdd:cd16226    33 SKERLGII---VDKIDKNGDGFVTEEELKDWIKYVQKKY----IREDVDRQWKEYDPNKDGKLSWEEYkkaTYGFLDDEE 105

                          90
                  ....*....|....*..
gi 1717014095 155 SDIAK--TFRKAINRKE 169
Cdd:cd16226   106 EDDDLheSYKKMIRRDE 122
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 88-154 7.75e-04

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


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 40.65  E-value: 7.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095  88 AFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRLmadgdKNKDGKIGFDEFVYIFQELKS 154
Cdd:cd16196    76 VFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVLRY-----SNKDGRISFDDFIMCAVKLKT 137
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 193-303 8.63e-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: 40.04  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKLTPFtiqENLNLALNSA 272
Cdd:cd21317    32 QKKTFTKWVN---------SHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21317   100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 579-690 8.82e-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: 39.56  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 579 EDLGDGQKVN-DDIIVRWVNRTLAEAGKStSIQSFKDKtISTSWAVVDLIDAIQPGCINYDLVKI----GDLSEDDKHDN 653
Cdd:cd21328     6 ETLEDLMKLSpEELLLRWANFHLENAGWQ-KINNFSSD-IKDSRAYFHLLNQIAPKGQKEGEPRIdinmSGFNEKDDLKR 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717014095 654 AKFAVSMARRIGARVYALPEDLVEVKPKMVMTVFACL 690
Cdd:cd21328    84 AEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 80-172 8.86e-04

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 40.65  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  80 DELEELREAFARVDLDNSGFISDYELHDLFKEAnlplpGYKVREIIQRLMADGDKNKDGKIGFDEFVYIFQELKSsdIAK 159
Cdd:cd16195    70 KKLRKYKDIFQKADVSKSGFLSLSELRNAIQAA-----GIRVSDDLLNLMALRYGDSSGRISFESFICLMLRLEC--MAK 142

                          90
                  ....*....|...
gi 1717014095 160 TFRKAINRKEGIC 172
Cdd:cd16195   143 IFRNLSKDGGGIY 155
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-183 8.96e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  83 EELREAFARVDLDNSGFISDYELHDLFkeanlplpgykvREIIQRLMADGDKNKDGKIGFDEFV----YIFQELKSSDIA 158
Cdd:COG5126     5 RKLDRRFDLLDADGDGVLERDDFEALF------------RRLWATLFSEADTDGDGRISREEFVagmeSLFEATVEPFAR 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717014095 159 KTFRKA-------INRKE---GICAIGGTSELSSE 183
Cdd:COG5126    73 AAFDLLdtdgdgkISADEfrrLLTALGVSEEEADE 107
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 194-250 9.00e-04

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: 39.32  E-value: 9.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095 194 KYAFVNWINKALENDpdcqhvLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERV 250
Cdd:cd21203     2 RYEAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPKVV 52
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 336-446 1.03e-03

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 39.20  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 336 SPEELLLRWANFHLENAGWNKINNFSSDIKDSRayfhLLNQIAPKgqkegeERID-INMSGFSEKDDLKRAEYMLQQADR 414
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGR----LFNAIIHK------YRPDlIDMNTVAVQSNLANLEHAFYVAEK 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717014095 415 LGCRQFVTPADVVSGNP--KLNLAFVANLFNKYP 446
Cdd:cd21239    71 LGVTRLLDPEDVDVSSPdeKSVITYVSSLYDVFP 104
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 337-431 1.42e-03

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 38.60  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 337 PEELLLRWANFHLENAGWNKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEeridinmsgFSEKDDLKRAEYMLQQADR-L 415
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAA---------IEQMDAEARLNLAFDFAEKkL 71

                          90
                  ....*....|....*.
gi 1717014095 416 GCRQFVTPADVVSGNP 431
Cdd:cd21226    72 GIPKLLEAEDVMTGNP 87
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 193-303 2.06e-03

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 38.24  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMIN-LSVPDTidERVINKKKLTPFTIQENLNLALNS 271
Cdd:cd21228     5 QQNTFTRWCN---------EHLKCVNKRIYNLETDLSDGLRLIALLEvLSQKRM--YKKYNKRPTFRQMKLENVSVALEF 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717014095 272 ASAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21228    74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLI 105
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 83-149 2.20e-03

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 40.41  E-value: 2.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717014095  83 EELREAFARVDLDNSGFISDYELHDLFK---EANLPLPGYKVREIIQR-LMADGDKNKDGKIGFDEFVYIF 149
Cdd:cd15902   181 EDFEKVFEHYDKDNNGVIEGNELDALLKdllEKNKADIDKPDLENFRDaILRACDKNKDGKIQKTELALFL 251
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 222-276 2.41e-03

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 38.47  E-value: 2.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1717014095 222 NDLF-KAVGDGIVLCKMINLSVPDTIdeRVINKKKlTPFTIQENLNLALNSASAIG 276
Cdd:cd21208    19 SDDFrESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 590-685 2.68e-03

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 37.99  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 590 DIIVRWVNRTLAEAgkstSIQSFkdktiSTSW----AVVDLIDAIQPG-CINYDlvkigDLSEDDKHDNAKFAVSMA-RR 663
Cdd:cd21184     4 SLLLEWVNSKIPEY----KVKNF-----TTDWndgkALAALVDALKPGlIPDNE-----SLDKENPLENATKAMDIAeEE 69

                          90       100
                  ....*....|....*....|....
gi 1717014095 664 IGARVYALPEDLV--EVKPKMVMT 685
Cdd:cd21184    70 LGIPKIITPEDMVspNVDELSVMT 93
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 84-111 2.81e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 2.81e-03
                           10        20
                   ....*....|....*....|....*...
gi 1717014095   84 ELREAFARVDLDNSGFISDYELHDLFKE 111
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 85-152 3.07e-03

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 38.73  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  85 LREAFARVDLDNSGFISDYELHDLFKEANlplPGYKVREIIQRL--MADGDKNKDGKIGFDEFVYIFQEL 152
Cdd:cd16206     2 LESVFEEADTNKSGFLDEEEAVQLIKQLN---PGLSTSRIKQKLkeLQKKKDGARGRVSSDEFVELFKEL 68
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 467-572 4.38e-03

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: 38.03  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 467 EERTFRNWMNS-----------LGVKPHVNHLYSDLQDALVILQLYEKiKVP--VD---WNKVNKPPYpklganmKKLEN 530
Cdd:cd21292    25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINL-SVPdtIDeraINKKKLTVF-------TIHEN 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1717014095 531 CNYAVD----LGkypakFSLVGIGGQDLNDGNSTLTLALVWQLMRR 572
Cdd:cd21292    97 LTLALNsasaIG-----CNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 200-276 4.41e-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: 37.29  E-value: 4.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095 200 WInKALENDPdcqhvLPMNPNTNDLFKavgDGIVLCKMINLSVPDTIdeRVINKKKLtPFTIQENLNLALNSASAIG 276
Cdd:cd21207    13 WI-EAVTGEK-----LDDGKDYEDVLK---DGVILCKLINILKPGSV--KKINTSKM-AFKLMENIENFLTACKGYG 77
S-100A10_like cd05031
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ...
 68-146 4.44e-03

S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.


Pssm-ID: 240157 [Multi-domain]  Cd Length: 94  Bit Score: 37.02  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  68 FHKMA----NTAQISKDELEELREAfarvdldnsgfisdyELHDLFKEANLPLpgykvreIIQRLMADGDKNKDGKIGFD 143
Cdd:cd05031    14 FHRYAgkdgDKNTLSRKELKKLMEK---------------ELSEFLKNQKDPM-------AVDKIMKDLDQNRDGKVNFE 71


                  ...
gi 1717014095 144 EFV 146
Cdd:cd05031    72 EFV 74
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 454-571 4.47e-03

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 38.07  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 454 QDIDWTLLEGETREERTFRNWMNS-----------LGVKPHVNHLYSDLQDALVILQLYeKIKVP--VDWNKVNKPPYPK 520
Cdd:cd21324    12 QSSAGTQHSYSEEEKYAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMI-NFSVPdtIDERTINKKKLTP 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717014095 521 LGANmkklENCNYAVDLGKyPAKFSLVGIGGQDLNDGNSTLTLALVWQLMR 571
Cdd:cd21324    91 FTIQ----ENLNLALNSAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 468-571 4.94e-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: 36.93  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 468 ERTFRNWMNS-LGVKPH--VNHLYSDLQDALVILQLYEKIK---VPVDWNKVNKPpypklganMKKLENCNYAVDLGKYP 541
Cdd:cd00014     1 EEELLKWINEvLGEELPvsITDLFESLRDGVLLCKLINKLSpgsIPKINKKPKSP--------FKKRENINLFLNACKKL 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 542 AKFSLVGIGGQDL-NDGNSTLTLALVWQLMR 571
Cdd:cd00014    73 GLPELDLFEPEDLyEKGNLKKVLGTLWALAL 103
PTZ00183 PTZ00183
centrin; Provisional
 70-148 5.04e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.13  E-value: 5.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717014095  70 KMANtaqisKDELEELREAFARVDLDNSGFISDYELHDLFKEANLPLPGYKVREIIQRlmadGDKNKDGKIGFDEFVYI 148
Cdd:PTZ00183   82 KLGE-----RDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDE----ADRNGDGEISEEEFYRI 151
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 64-145 5.11e-03

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: 37.12  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  64 YTSQFHKMANTaQISKDELEELREAFARVDLDNSGFISDYELHDLFKEA-----NLPLPGYKVREIIQRLMADGdknkDG 138
Cdd:cd16252    19 YSKFFEYMQKF-QTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVpssmpVAPLSDEEAEAMIQAADTDG----DG 93


                  ....*..
gi 1717014095 139 KIGFDEF 145
Cdd:cd16252    94 RIDFQEF 100
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 193-303 5.25e-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: 38.10  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINkalendpdcQHVLPMNPNTNDLFKAVGDGIVLCKMINLSVPDTIDERVINKKKLTPFtiqENLNLALNSA 272
Cdd:cd21316    54 QKKTFTKWVN---------SHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21316   122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 84-154 5.59e-03

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 38.18  E-value: 5.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717014095  84 ELREAFARVDLDnSGFISDYELHDLFKEANLPLPGYKVR-EIIQRLMADGDKNKDGKIGFDEFVYIFQELKS 154
Cdd:cd15897     1 QLRNVFQAVAGD-DGEISATELQQALSNVGWTHFDLGFSlETCRSMIAMMDRDHSGKLNFSEFKGLWNYIKA 71
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 220-276 5.98e-03

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 36.96  E-value: 5.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1717014095 220 NTNDLFKAVGDGIVLCKMINLSVPDTIdeRVINKKKLtPFTIQENLNLALNSASAIG 276
Cdd:cd21210    18 AQGDLLDALKDGVVLCKLANRILPADI--RKYKESKM-PFVQMENISAFLNAARKLG 71
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 124-152 6.44e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.68  E-value: 6.44e-03
                          10        20
                  ....*....|....*....|....*....
gi 1717014095 124 IIQRLMADGDKNKDGKIGFDEFVYIFQEL 152
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 84-111 7.40e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 7.40e-03
                          10        20
                  ....*....|....*....|....*...
gi 1717014095  84 ELREAFARVDLDNSGFISDYELHDLFKE 111
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_PEF_CAPN2 cd16199
Penta-EF hand, calcium binding motifs, found in m-type calpain (CAPN2); CAPN2, also termed ...
 81-181 8.18e-03

Penta-EF hand, calcium binding motifs, found in m-type calpain (CAPN2); CAPN2, also termed millimolar-calpain (m-calpain), or calpain-2 catalytic subunit, or calcium-activated neutral proteinase 2 (CANP 2), or calpain large polypeptide L2, or calpain-2 large subunit, is a ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine protease that contains 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 catalytic subunit CAPN2 in complex with a regulatory subunit encoded by CAPNS1 forms an m-calpain heterodimer. CAPN2 acts as the key protease responsible for N-methyl-d-aspartic acid (NMDA)-induced cytoplasmic polyadenylation element-binding protein 3 (CPEB3) degradation in neurons. It cleaves several components of the focal adhesion complex, such as FAK and talin, triggering disassembly of the complex at the rear of the cell. The stimulation of CAPN2 activity is required for Golgi antiapoptotic proteins (GAAPs) to promote cleavage of FA kinase (FAK), cell spreading, and enhanced migration. calpain 2 is also involved in the onset of glial differentiation. It regulates proliferation, survival, migration, and tumorigenesis of breast cancer cells through a PP2A-Akt-FoxO-p27(Kip1) signaling cascade. Its expression is associated with response to platinum based chemotherapy, progression-free and overall survival in ovarian cancer. Moreover, CAPN2 may play a role in fundamental mitotic functions, such as the maintenance of sister chromatid cohesion. The activation of CAPN2 plays an essential role in hippocampal synaptic plasticity and in learning and memory. In the eye, CAPN2, together with a lens-specific variant of CAPN3, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. Sometimes, CAPN2 compensates for loss of CAPN1, and both calpain isoforms are involved in AngII-induced aortic aneurysm formation. The main phosphorylation sites in m-calpain are Ser50 and Ser369/Thr370.


Pssm-ID: 320074 [Multi-domain]  Cd Length: 168  Bit Score: 37.96  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  81 ELEELREAFARVDLDNSGFISDYELHDLFKEANLPLPGyKVREIIQRLMADGDKNkdgkIGFDEFVYIFQELKSsdIAKT 160
Cdd:cd16199    71 KIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPC-QLHQVIVARFADDDLI----IDFDNFVRCLVRLET--LFKI 143

                          90       100
                  ....*....|....*....|.
gi 1717014095 161 FRKAINRKEGICAIGGTSELS 181
Cdd:cd16199   144 FKQLDPENTGTIELDLISWLS 164
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 193-303 8.54e-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: 36.53  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095 193 EKYAFVNWINKALENDPdcqhvlpmNPNTNDLFKAVGDGIvlcKMINLsVPDTIDERVINKKKLTPFTIQENLNLALNSA 272
Cdd:cd21232     3 QKKTFTKWINARFSKSG--------KPPIKDMFTDLRDGR---KLLDL-LEGLTGKSLPKERGSTRVHALNNVNRVLQVL 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717014095 273 SAIGCHVVNIGAEDLKAGKPHLVLGLLWQII 303
Cdd:cd21232    71 HQNNVELVNIGGTDIVDGNHKLTLGLLWSII 101
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 74-169 9.79e-03

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 38.32  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717014095  74 TAQISKDELEELREafaRVDLDNSGFISDYELHDLFKEANlplpGYKVREIIQRLMADGDKNKDGKIGFDEF------VY 147
Cdd:cd16229    29 TPEESKERLGKIVD---RIDDDKDGFVTTEELKAWIKRVQ----KRYIYENVAKVWKDYDLNKDNKISWEEYkqatygYY 101

                          90       100
                  ....*....|....*....|....
gi 1717014095 148 IFQELKSSDIAK--TFRKAINRKE 169
Cdd:cd16229   102 LGNPEEFQDATDqfSFKKMLPRDE 125
 
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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