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Conserved domains on  [gi|31543113|ref|NP_032905|]
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plastin-2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-620 3.89e-79

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401  Cd Length: 612  Bit Score: 265.65  E-value: 3.89e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  16 EAFAKVDTDGNGYISCNELNDLFKAACL----PLPgYRVREITENLmatgdldqDGKISFDEFIkvfhGLKSTEVAKTFR 91
Cdd:COG5069  28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENV--------SGRLEFIKGK----GVKLFNIGPQDI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  92 KAINKKEGIcaiGGTSEQSSVGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFNAVGDGIVLCKMINLSV 171
Cdd:COG5069  95 VDGNPKLIL---GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 172 PDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIELSRNE 246
Cdd:COG5069 169 PDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIALHR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 247 aLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavvidmsGLR 326
Cdd:COG5069 245 -VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA----------PLE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 327 EKDDIQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPAL------HKPENQDIDwgaLEGEtREERTF 400
Cdd:COG5069 313 TTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 401 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVDLGKNQAkFSLVG 477
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 478 IAGQDLNEGNRtLTLALVWQLMRRYTLNILEDIG-GGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLP-VLDL 555
Cdd:COG5069 464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543113 556 IDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVNPKM-VMTVFACLM 620
Cdd:COG5069 543 LKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-620 3.89e-79

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


Pssm-ID: 227401  Cd Length: 612  Bit Score: 265.65  E-value: 3.89e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  16 EAFAKVDTDGNGYISCNELNDLFKAACL----PLPgYRVREITENLmatgdldqDGKISFDEFIkvfhGLKSTEVAKTFR 91
Cdd:COG5069  28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENV--------SGRLEFIKGK----GVKLFNIGPQDI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  92 KAINKKEGIcaiGGTSEQSSVGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFNAVGDGIVLCKMINLSV 171
Cdd:COG5069  95 VDGNPKLIL---GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 172 PDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIELSRNE 246
Cdd:COG5069 169 PDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIALHR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 247 aLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavvidmsGLR 326
Cdd:COG5069 245 -VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA----------PLE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 327 EKDDIQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPAL------HKPENQDIDwgaLEGEtREERTF 400
Cdd:COG5069 313 TTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 401 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVDLGKNQAkFSLVG 477
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 478 IAGQDLNEGNRtLTLALVWQLMRRYTLNILEDIG-GGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLP-VLDL 555
Cdd:COG5069 464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543113 556 IDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVNPKM-VMTVFACLM 620
Cdd:COG5069 543 LKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
121-236 5.88e-23

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 95.46  E-value: 5.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 121 EEKYAFVNWINKALENDPDcrhvipmnPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKkkLTPFTIQENLNLALNS 200
Cdd:cd00014   1 SQKEELLRWINKVLGEYGP--------VTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP--LSRFKRLENINLALNF 70
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31543113 201 ASAIGCHVVNIGAEDL-KEGKPYLVLGLLWQVIKIGL 236
Cdd:cd00014  71 AEKLGVPVVNFDAEDLvEDGDEKLVLGLLWSLIRKFL 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
120-235 4.83e-22

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


Pssm-ID: 306753  Cd Length: 109  Bit Score: 93.12  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   120 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKkltPFTIQENLNLALN 199
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDYKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 31543113   200 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 235
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
124-234 4.71e-21

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 90.07  E-value: 4.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113    124 YAFVNWINKALENDPdcrhvipmNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 203
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 31543113    204 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 234
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
PTZ00183 PTZ00183
centrin; Provisional
2-77 1.85e-06

centrin; Provisional


Pssm-ID: 185503  Cd Length: 158  Bit Score: 48.15  E-value: 1.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543113    2 ARGSVSDEEMMELREAFAKVDTDGNGYISCNElndlFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00183   7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-620 3.89e-79

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


Pssm-ID: 227401  Cd Length: 612  Bit Score: 265.65  E-value: 3.89e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  16 EAFAKVDTDGNGYISCNELNDLFKAACL----PLPgYRVREITENLmatgdldqDGKISFDEFIkvfhGLKSTEVAKTFR 91
Cdd:COG5069  28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENV--------SGRLEFIKGK----GVKLFNIGPQDI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  92 KAINKKEGIcaiGGTSEQSSVGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFNAVGDGIVLCKMINLSV 171
Cdd:COG5069  95 VDGNPKLIL---GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 172 PDTIDERTINK----KKLTPFTIQENLNLALNSASAIG-CHVVNIGAEDLKEGKPYLVlgllWQVIKIGLFADIELSRNE 246
Cdd:COG5069 169 PDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERSIMTYVS----WYIIRFGLLEKIDIALHR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 247 aLIALLREGESLEDlMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavvidmsGLR 326
Cdd:COG5069 245 -VYRLLEADETLIQ-LRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRA----------PLE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 327 EKDDIQRAECMLQQAERLGCRQFVTATdvvrGNPKLNLAFIANLFNKYPAL------HKPENQDIDwgaLEGEtREERTF 400
Cdd:COG5069 313 TTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 401 RNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVP--VDWNRVNKPPYPKLGGN-MKKLENCNYAVDLGKNQAkFSLVG 477
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVG 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 478 IAGQDLNEGNRtLTLALVWQLMRRYTLNILEDIG-GGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLP-VLDL 555
Cdd:COG5069 464 IKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDV 542
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543113 556 IDAIQPGSINYDLLKTENLDDEEKLNNAKYAIS--MARKIGARVYALPEDLVEVNPKM-VMTVFACLM 620
Cdd:COG5069 543 LKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
121-236 5.88e-23

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 95.46  E-value: 5.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 121 EEKYAFVNWINKALENDPDcrhvipmnPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKkkLTPFTIQENLNLALNS 200
Cdd:cd00014   1 SQKEELLRWINKVLGEYGP--------VTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP--LSRFKRLENINLALNF 70
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31543113 201 ASAIGCHVVNIGAEDL-KEGKPYLVLGLLWQVIKIGL 236
Cdd:cd00014  71 AEKLGVPVVNFDAEDLvEDGDEKLVLGLLWSLIRKFL 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
120-235 4.83e-22

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


Pssm-ID: 306753  Cd Length: 109  Bit Score: 93.12  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   120 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKkltPFTIQENLNLALN 199
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDYKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 31543113   200 SAS-AIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIG 235
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
264-376 2.28e-21

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


Pssm-ID: 306753  Cd Length: 109  Bit Score: 91.20  E-value: 2.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   264 LSPEELLLRWANYHLENAG-CTKITNFSTDIKDSKAYYHLLEQVAPKGDEEgipavviDMSGLREKDDIQRAECMLQQAE 342
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDY-------KKLNKSEFDKLENINLALDVAE 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 31543113   343 R-LGCRQF-VTATDVVRGNPKLNLAFIANLFNKYPA 376
Cdd:pfam00307  74 KkLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFPK 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
124-234 4.71e-21

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 90.07  E-value: 4.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113    124 YAFVNWINKALENDPdcrhvipmNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKlTPFTIQENLNLALNSASA 203
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 31543113    204 IGCHVVNIGAEDLKEGKPyLVLGLLWQVIKI 234
Cdd:smart00033  72 LGGKVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
518-625 1.09e-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: 306753  Cd Length: 109  Bit Score: 83.49  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   518 DDIIVNWVNTTLKEAQKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLKTENlddEEKLNNAKYAISMAR-KIGAR 596
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFTT-DLRDGLALCALLNKLAPGLVDYKKLNKSE---FDKLENINLALDVAEkKLGVP 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 31543113   597 VYAL-PEDLVEVNPKMVMTVFACLMGKGMK 625
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFPK 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
396-502 3.76e-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: 306753  Cd Length: 109  Bit Score: 81.95  E-value: 3.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   396 EERTFRNWMNSL----GVNPRVNHLYSDLSDALVIFQLYEKIKvP--VDWNRVNKPPypklggnMKKLENCNYAVDLGKN 469
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDYKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 31543113   470 QAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRY 502
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
265-375 4.22e-18

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 81.97  E-value: 4.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 265 SPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAvvidmsGLREKDDIQRAECMLQQAERL 344
Cdd:cd00014   1 SQKEELLRWINKVLGEYGPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKIN------PLSRFKRLENINLALNFAEKL 74
                        90       100       110
                ....*....|....*....|....*....|...
gi 31543113 345 GCRQF-VTATDVV-RGNPKLNLAFIANLFNKYP 375
Cdd:cd00014  75 GVPVVnFDAEDLVeDGDEKLVLGLLWSLIRKFL 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
268-373 9.83e-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  Cd Length: 101  Bit Score: 74.66  E-value: 9.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113    268 ELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKgdeeGIPAVVIDMSGLREKdDIQRAECMLQQAERLGC- 346
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPG----LVDKKKVAASLSRFK-KIENINLALSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*..
gi 31543113    347 RQFVTATDVVRGnPKLNLAFIANLFNK 373
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-501 3.54e-15

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 73.12  E-value: 3.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113    398 RTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKVP-VDWNRVNKPPYPklggnMKKLENCNYAVDLGKNQaKF 473
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEKL-GG 74
                           90       100
                   ....*....|....*....|....*...
gi 31543113    474 SLVGIAGQDLNEGNRtLTLALVWQLMRR 501
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
13-79 1.14e-13

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  Cd Length: 63  Bit Score: 67.96  E-value: 1.14e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
519-620 5.08e-13

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.96  E-value: 5.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113    519 DIIVNWVNTTLKEAqKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDLLkTENLDDEEKLNNAKYAISMARKIG-ARV 597
Cdd:smart00033   1 KTLLRWVNSLLAEY-DKPPVTNFSS-DLKDGVALCALLNSLSPGLVDKKKV-AASLSRFKKIENINLALSFAEKLGgKVV 77
                           90       100
                   ....*....|....*....|...
gi 31543113    598 YALPEDLVEVnPKMVMTVFACLM 620
Cdd:smart00033  78 LFEPEDLVEG-PKLILGVIWTLI 99
EF-hand_7 pfam13499
EF-hand domain pair;
13-78 6.09e-10

EF-hand domain pair;


Pssm-ID: 316058  Cd Length: 68  Bit Score: 57.28  E-value: 6.09e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543113    13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITEnLMATGDLDQDGKISFDEFIKVF 78
Cdd:pfam13499   3 KLKEAFKLLDKDGDGYLDVEELKKLLRKLFEEGEKLSDEEVEE-LFKEFDLDKDGRISFEEFLELY 67
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
518-623 2.29e-08

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 53.47  E-value: 2.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 518 DDIIVNWVNTTLKEAqKSSSIASFKDpKISTSLPVLDLIDAIQPGSINYDllKTENLDDEEKLNNAKYAISMARKIGARV 597
Cdd:cd00014   3 KEELLRWINKVLGEY-GPVTINNFST-DLKDGIALCKLLNSLSPDLIDKK--KINPLSRFKRLENINLALNFAEKLGVPV 78
                        90       100
                ....*....|....*....|....*...
gi 31543113 598 YAL-PEDLVE-VNPKMVMTVFACLMGKG 623
Cdd:cd00014  79 VNFdAEDLVEdGDEKLVLGLLWSLIRKF 106
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
395-502 4.23e-07

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 49.62  E-value: 4.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113 395 REERTFRNWMNSL---GVNPRVNHLYSDLSDALVIFQLYEKIKvPvdwNRVNKPpYPKLGGNMKKLENCNYAVDLGKnQA 471
Cdd:cd00014   1 SQKEELLRWINKVlgeYGPVTINNFSTDLKDGIALCKLLNSLS-P---DLIDKK-KINPLSRFKRLENINLALNFAE-KL 74
                        90       100       110
                ....*....|....*....|....*....|..
gi 31543113 472 KFSLVGIAGQDL-NEGNRTLTLALVWQLMRRY 502
Cdd:cd00014  75 GVPVVNFDAEDLvEDGDEKLVLGLLWSLIRKF 106
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
16-77 1.59e-06

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


Pssm-ID: 320075  Cd Length: 254  Bit Score: 49.66  E-value: 1.59e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543113  16 EAFAKVDTDGNGYISCNELNDLFKAACLPLPG-----YRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:cd15902   3 EVWMHFDADGNGYIEGKELDSFLRELLKALNGkdktdDEVAEKKKEFMEKYDENEDGKIEIRELANI 69
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
13-74 1.80e-06

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


Pssm-ID: 320060  Cd Length: 163  Bit Score: 47.98  E-value: 1.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLpGYRVreiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16185   1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLF-SLAT---AEKLIRMFDRDGNGTIDFEEF 58
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
13-83 1.82e-06

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


Pssm-ID: 320055  Cd Length: 164  Bit Score: 48.29  E-value: 1.82e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAAClplpGYRVREITENLMATG-DLDQDGKISFDEFIKVFHGLKS 83
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALSNGD----WTPFSIETVRLMINMfDRDRSGTINFDEFVGLWKYIQD 68
PTZ00183 PTZ00183
centrin; Provisional
2-77 1.85e-06

centrin; Provisional


Pssm-ID: 185503  Cd Length: 158  Bit Score: 48.15  E-value: 1.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543113    2 ARGSVSDEEMMELREAFAKVDTDGNGYISCNElndlFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00183   7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
PTZ00184 PTZ00184
calmodulin; Provisional
1-77 7.36e-06

calmodulin; Provisional


Pssm-ID: 185504  Cd Length: 149  Bit Score: 46.29  E-value: 7.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543113    1 MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVreitENLMATGDLDQDGKISFDEFIKV 77
Cdd:PTZ00184  73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV----DEMIREADVDGDGQINYEEFVKM 145
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
13-74 7.58e-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  Cd Length: 101  Bit Score: 45.60  E-value: 7.58e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16251  35 QIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRDLTDEE-TKALLAAGDTDGDGKIGVEEF 95
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
13-79 9.10e-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  Cd Length: 101  Bit Score: 45.58  E-value: 9.10e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREiTENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd16254  35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSDKE-TKALLAAGDKDGDGKIGIDEFATLVA 100
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-77 1.22e-05

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


Pssm-ID: 227455  Cd Length: 160  Bit Score: 45.76  E-value: 1.22e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543113   7 SDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGyrvREITEnLMATGDlDQDGKISFDEFIKV 77
Cdd:COG5126  15 TEEQIQELKEAFQLFDRDSDGLIDRNELGKILRSLGFNPSE---AEINK-LFEEID-AGNETVDFPEFLTV 80
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-78 1.51e-05

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


Pssm-ID: 227455  Cd Length: 160  Bit Score: 45.38  E-value: 1.51e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543113   1 MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITeNLMatgDLDQDGKISFDEFIKVF 78
Cdd:COG5126  81 MSVKLKRGDKEEELREAFKLFDKDHDGYISIGELRRVLKSLGERLSDEEVEKLL-KEY---DEDGDGEIDYEEFKKLI 154
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
13-74 1.54e-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  Cd Length: 101  Bit Score: 44.86  E-value: 1.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAAClplPGYRV---REiTENLMATGDLDQDGKISFDEF 74
Cdd:cd16253  35 DIKKVFNILDQDKSGFIEEEELKLFLKNFS---DGARVlsdKE-TKNFLAAGDSDGDGKIGVDEF 95
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
7-98 2.38e-05

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


Pssm-ID: 320024  Cd Length: 264  Bit Score: 46.42  E-value: 2.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   7 SDEEMME-LREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyRVREITENLMATGDLDQDGKISFDEFIKVFHG----- 80
Cdd:cd16226  29 TPEESKErLGIIVDKIDKNGDGFVTEEELKDWIKYVQKK----YIREDVDRQWKEYDPNKDGKLSWEEYKKATYGfldde 104
                        90
                ....*....|....*...
gi 31543113  81 LKSTEVAKTFRKAINKKE 98
Cdd:cd16226 105 EEDDDLHESYKKMIRRDE 122
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
7-76 3.85e-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  Cd Length: 254  Bit Score: 45.42  E-value: 3.85e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543113   7 SDEEMMElreAFAKVDTDGNGYISCNEL----NDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIK 76
Cdd:cd15902  88 SSVEFMK---IWRKYDTDGSGFIEAKELkgflKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
13-100 5.39e-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  Cd Length: 167  Bit Score: 43.75  E-value: 5.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAAclplpGYRV-REITENLM---AtgdlDQDGKISFDEFIKVFHGLKSteVAK 88
Cdd:cd16182  73 KWQAIFKKFDTDRSGTLSSYELRKALESA-----GFHLsNKVLQALVlryA----DSTGRITFEDFVSCLVRLKT--AFE 141
                        90
                ....*....|..
gi 31543113  89 TFRKAINKKEGI 100
Cdd:cd16182 142 TFSALDKKNEGV 153
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
13-79 6.46e-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  Cd Length: 101  Bit Score: 42.80  E-value: 6.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNdLFkaacLPLPGYRVREITEN----LMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd16255  35 DVKKVFEIIDQDKSGFIEEEELK-LF----LQNFSSGARELTDAetkaFLKAGDSDGDGKIGVEEFQALVK 100
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
15-77 6.58e-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  Cd Length: 164  Bit Score: 43.67  E-value: 6.58e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543113  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRV-REITENLMATGDLDQDGKISFDEFIKV 77
Cdd:cd16180  70 RRLFRRFDRDRSGSIDFNELQNALSSF-----GYRLsPQFVQLLVRKFDRRRRGSISFDDFVEA 128
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
13-84 9.58e-05

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


Pssm-ID: 320077  Cd Length: 248  Bit Score: 44.10  E-value: 9.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  13 ELREAFAKVDTDGNGYISCNE----LNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDE----------FIKVF 78
Cdd:cd16177  91 EFMEAWRKYDTDRSGYIEANElkgfLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEmarllpvqenFLLKF 170

                ....*.
gi 31543113  79 HGLKST 84
Cdd:cd16177 171 QGMKLS 176
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
4-75 1.34e-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  Cd Length: 167  Bit Score: 42.57  E-value: 1.34e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543113   4 GSVSDEEMMEL-------REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFI 75
Cdd:cd16196  56 GKLGFEEFKKLwedlrswKRVFKLFDTDGSGSFSSFELRNALNSA-----GFRLSNATLNALVLRYSNKDGRISFDDFI 129
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
13-90 2.29e-04

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


Pssm-ID: 320054  Cd Length: 165  Bit Score: 42.03  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  13 ELREAFAKVDTDgNGYISCNELNDLFKAACLPLPGYRVR-EITENLMATGDLDQDGKISFDEFIKVFHGLKS-TEVAKTF 90
Cdd:cd15897   1 QLRNVFQAVAGD-DGEISATELQQALSNVGWTHFDLGFSlETCRSMIAMMDRDHSGKLNFSEFKGLWNYIKAwQEIFRTY 79
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
1-74 2.58e-04

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


Pssm-ID: 319995  Cd Length: 106  Bit Score: 40.98  E-value: 2.58e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543113   1 MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVR-EITENLMATGDLDQDGKISFDEF 74
Cdd:cd16252  26 MQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVAPLSdEEAEAMIQAADTDGDGRIDFQEF 100
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
14-100 3.43e-04

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


Pssm-ID: 320029  Cd Length: 137  Bit Score: 41.11  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  14 LREAFAKVDTDGNGYISCNELNDLFKAACLPLPgyrvREITENLMATGDLDQDGKISFDEFIKVFHGLKST-EVAKTFRK 92
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVS----EKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERpELEPIFKK 77

                ....*....
gi 31543113  93 -AINKKEGI 100
Cdd:cd15898  78 yAGTNRDYM 86
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
15-78 4.91e-04

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


Pssm-ID: 320054  Cd Length: 165  Bit Score: 40.88  E-value: 4.91e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543113  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:cd15897  73 QEIFRTYDTDGSGTIDSNELRQALSGA-----GYRLSEQTYDIIIRRYDRGRGNIDFDDFIQCC 131
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
16-79 8.12e-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  Cd Length: 67  Bit Score: 39.13  E-value: 8.12e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543113  16 EAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:cd00052   3 QIFRSLDPDGDGLISGDEARPFLGKSGLP------RSVLAQIWDLADTDKDGKLDKEEFAIAMH 60
EF-hand_6 pfam13405
EF-hand domain;
13-40 9.08e-04

EF-hand domain;


Pssm-ID: 315968  Cd Length: 30  Bit Score: 38.71  E-value: 9.08e-04
                          10        20
                  ....*....|....*....|....*...
gi 31543113    13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGYISLEELRKALRS 28
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
6-79 1.00e-03

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


Pssm-ID: 197477  Cd Length: 96  Bit Score: 39.18  E-value: 1.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543113      6 VSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPlpgyrvREITENLMATGDLDQDGKISFDEFIKVFH 79
Cdd:smart00027   4 ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLP------QTLLAKIWNLADIDNDGELDKDEFALAMH 71
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
13-40 1.09e-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: 306533  Cd Length: 29  Bit Score: 38.54  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*...
gi 31543113    13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
14-93 1.73e-03

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


Pssm-ID: 320032  Cd Length: 140  Bit Score: 38.75  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113  14 LREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREItenLMATgDLDQDGKISFDEFIKVFHGL-KSTEVAKTFRK 92
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKL---FQEA-DTSGEDVLDEEEFVQFYNRLtKRPEIEELFKK 77

                .
gi 31543113  93 A 93
Cdd:cd16202  78 Y 78
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
13-40 2.55e-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  Cd Length: 29  Bit Score: 37.36  E-value: 2.55e-03
                           10        20
                   ....*....|....*....|....*...
gi 31543113     13 ELREAFAKVDTDGNGYISCNELNDLFKA 40
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
15-91 2.63e-03

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


Pssm-ID: 320059  Cd Length: 165  Bit Score: 38.78  E-value: 2.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543113  15 REAFAKVDTDGNGYISCNELNDLFKAAclplpGYRVR-EITENLMATGDLDQDGKISFDEFIKVFHGLKS-TEvakTFR 91
Cdd:cd16184  70 KQVFQQFDRDRSGSIDENELHQALSQM-----GYRLSpQFVQFLVSKYDPRARRSLTLDQFIQVCVQLQSlTD---AFR 140
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
4-75 3.66e-03

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


Pssm-ID: 320060  Cd Length: 163  Bit Score: 38.35  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543113   4 GSVSDEEMMEL-------REAFAKVDTDGNGYIscnELNDLFKAacLPLPGYRVREITEN-LMATGDLDQDGKISFDEFI 75
Cdd:cd16185  51 GTIDFEEFAALhqflsnmQNGFEQRDTSRSGRL---DANEVHEA--LAASGFQLDPPAFQaLFRKFDPDRGGSLGFDDYI 125
PLN02964 PLN02964
phosphatidylserine decarboxylase
5-73 3.94e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520  Cd Length: 644  Bit Score: 40.23  E-value: 3.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543113    5 SVSDEEMMELREAFAK-----VDTDGNGYISCNELNDLFKAAclplpGYRVR-EITENLMATGDLDQDGKISFDE 73
Cdd:PLN02964 167 SCSIEDPVETERSFARrilaiVDYDEDGQLSFSEFSDLIKAF-----GNLVAaNKKEELFKAADLNGDGVVTIDE 236
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
18-78 4.72e-03

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


Pssm-ID: 320078  Cd Length: 257  Bit Score: 38.92  E-value: 4.72e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543113  18 FAKV----DTDGNGYISCNELNDLFKAACLPLPGY------RVREITENLMATGDLDQDGKISFDEFIKVF 78
Cdd:cd16178   1 FAEIwqhfDADESGYIEGKELDNFFKDLLKKLGTKdtisadEVQDVKECFMSAYDVTGDGRIQIQELANII 71
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
17-85 5.94e-03

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


Pssm-ID: 320063  Cd Length: 169  Bit Score: 37.80  E-value: 5.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543113  17 AFAKVDTDGNGYISCNELNDLFKAAclplpGYRVREITENLMATGDLDQDGKISFDEFIK-------VFHGLKSTE 85
Cdd:cd16188  78 IYKQFDTDRSGTIGSQELPGAFEAA-----GFHLNEQLYQMIIRRYSDEDGNMDFDNFISclvrldaMFRAFKSLD 148
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
13-73 6.59e-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  Cd Length: 254  Bit Score: 38.49  E-value: 6.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543113  13 ELREAFAKVDTDGNGYISCNELNDLFKAAC---LPLPGYRVRE-ITENLMATGDLDQDGKISFDE 73
Cdd:cd15902 182 DFEKVFEHYDKDNNGVIEGNELDALLKDLLeknKADIDKPDLEnFRDAILRACDKNKDGKIQKTE 246
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
18-78 7.34e-03

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


Pssm-ID: 320009  Cd Length: 107  Bit Score: 36.58  E-value: 7.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543113  18 FAKVDTDGNGYISCNELnDLFKAACLPLpGYRVREITEnlmaTGDLDQDGKISFDEFIKVF 78
Cdd:cd00252  51 FDNLDNNKDGKLDKREL-APFRAPLMPL-EHCARGFFE----SCDLNKDKKISLQEWLGCF 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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