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Conserved domains on  [gi|1514903181|gb|ROI98699|]
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Fibrillin-3 [Anabarilius grahami]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
2540-2707 2.48e-102

calmodulin; Provisional


:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 324.41  E-value: 2.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2540 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD 2619
Cdd:PTZ00184     2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2620 SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftE 2699
Cdd:PTZ00184    82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYE--------------------E 141

                   ....*...
gi 1514903181 2700 FVQMMTAK 2707
Cdd:PTZ00184   142 FVKMMMSK 149
NIDO super family cl02648
Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found ...
1421-1557 1.54e-16

Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found in nidogen and hypothetical proteins of unknown function.


The actual alignment was detected with superfamily member smart00539:

Pssm-ID: 470642  Cd Length: 152  Bit Score: 79.01  E-value: 1.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1421 VFWDDADlTLGDGKLLYQEYSllnisDIYaekVFNRTAQDVSrfETQRGNPRFTPSWMVKITWDHVlpVSYQKINLSETN 1500
Cdd:smart00539    1 PFWADAD-TEGTGKVYYRETT-----DHA---ILDRATESVR--EGFTDMGGFRAKSVVIVTWENV--AAYGSQSSDGTN 67
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1514903181  1501 TFQCILTTDGLRSFALLRYSDMNW----GPGQRTDHNALIGYTDGKNNFHNEIPK----PPNNLF 1557
Cdd:smart00539   68 TFQAVLATDGSRTYAIFLYPSLGWtsdtTAGGDDGVRARAGFNGGDGTFSYTLPAsgeeNIKNLA 132
VWD super family cl47498
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1751-1920 4.17e-09

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


The actual alignment was detected with superfamily member pfam00094:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 57.77  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1751 VYGSLHFITFDGSEYTFKALGEYVIVRLSTSTGSniFTLQGQTAALVVNGQPKLVPALErlaaFYQGAGKVEwrcaeSGD 1830
Cdd:pfam00094    3 VSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVCLKSVT----VIVGDLEIT-----LQK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1831 GLKVLVNDVVIPVsvgvvHVEEKAFAVRCTSMSRCAVVYAEGLyVVVWRGDaGRLTALVEVPQRFYNRTLGLLGLWNSNR 1910
Cdd:pfam00094   72 GGTVLVNGQKVSL-----PYKSDGGEVEILGSGFVVVDLSPGV-GLQVDGD-GRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144
                          170
                   ....*....|
gi 1514903181 1911 TDDFLLSNGR 1920
Cdd:pfam00094  145 EDDFMTPDGT 154
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
138-173 4.40e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 53.76  E-value: 4.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  138 CQTNNGGCHVNALCTNRDGGRDCSCKSGFSGNGFQC 173
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
97-132 1.84e-08

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.22  E-value: 1.84e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181   97 CTTGLHSCHGKAICSNTLGSYTCSCLNGYFGDGFQC 132
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
544-583 1.25e-07

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 1.25e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   544 DIDECENQKPCHQNGTCLNLAGSFSCTCKHGFSgNGVTCE 583
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
181-210 3.86e-07

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 48.36  E-value: 3.86e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181  181 RPGICHWNATCTNNPGSYVCTCNAGYKGNG 210
Cdd:pfam12947    4 NNGGCHPNATCTNTGGSFTCTCNDGYTGDG 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
299-338 1.02e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.25  E-value: 1.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  299 DINECDRKNNCDPNAICTNLLGSYQCSCRSGFlgTGTKCT 338
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
951-990 1.13e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 1.13e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   951 DINECSQSGACPKLSTCFNTEGSYHCDCWEGYQyNGIHCE 990
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
1286-1320 1.48e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 46.82  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181 1286 CAKNTT-CHPLARCWNTVGSFTCQCRLGYAGNGTYC 1320
Cdd:pfam12947    1 CSDNNGgCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1242-1275 3.09e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 3.09e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181  1242 DINECLSNRTCRPDQVCINKPGSYQCSCPLGHHE 1275
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTD 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
339-370 3.87e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 3.87e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181   339 DIDECAASNICPSNAVCVNTAGSFFCDCGQGY 370
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
837-868 4.18e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 45.28  E-value: 4.18e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  837 PHNCSLLAMCNNTEGSYICKCMEGYLGDGFTC 868
Cdd:pfam12947    5 NGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1074-1110 4.40e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 4.40e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1514903181  1074 DVDECLNNSACSDNSICVNTEGSFLCLCDDGFSSNGT 1110
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
789-824 1.02e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.51  E-value: 1.02e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  789 CQSQHGGCHPAASCTNSPGSYKCTCPFGMNGSGFDC 824
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
260-298 1.23e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 1.23e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   260 DINECE-INICSSFADCTNLPGSYRCTCPEGFVgNGLACV 298
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
870-900 2.60e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 2.60e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1514903181   870 DVDECLSPSICRNNMTCQNFPGTYTCTCTVG 900
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1158-1197 5.27e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.27e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181  1158 DIDECSGSNNesiCQPHSTCVNVPGSYKCDCNLGFLLNRT 1197
Cdd:smart00179    1 DIDECASGNP---CQNGGTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
459-492 5.76e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 5.76e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   459 DVNECLvDNGGCRNRAKCVNSMGSFSCTCPSGFQ 492
Cdd:smart00179    1 DIDECA-SGNPCQNGGTCVNTVGSYRCECPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
428-454 7.12e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.12e-05
                           10        20
                   ....*....|....*....|....*..
gi 1514903181  428 CHVNALCINVPGKFNCSCMVGYTGDGV 454
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGV 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
592-622 7.41e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.41e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1514903181  592 GMCHLQANCYNYPGEFMCICHQGFNGDGFTC 622
Cdd:pfam12947    6 GGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1322-1353 9.32e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 9.32e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181  1322 DIDECSTSSLrCHKSSQCINTPGSYICVCAPG 1353
Cdd:smart00179    1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPG 31
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
748-783 1.04e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.43  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  748 CESGVNSCSKFAQCDNTIGSHLCFCLNGFTGDGKNC 783
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
1033-1064 1.63e-04

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1033 DVDECATGKAQCPNASNCQNTVGWYFCECWDG 1064
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
1117-1156 3.34e-04

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.34e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1117 DIDECidEFGPLCTNG-TCINTIGSFHCVCDMGFwSNDTRC 1156
Cdd:smart00179    1 DIDEC--ASGNPCQNGgTCVNTVGSYRCECPPGY-TDGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
379-416 3.51e-04

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.51e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1514903181   379 DVDECAIRH-CSPYSSCENLPGSFICSCIAGFEgDGLIC 416
Cdd:smart00179    1 DIDECASGNpCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA pfam07645
Calcium-binding EGF domain;
991-1019 4.85e-04

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.85e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  991 DINECSVGNFICPDNSTCYNKEGGYNCPC 1019
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA pfam07645
Calcium-binding EGF domain;
2369-2397 4.94e-04

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.94e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181 2369 DLDECKTNEAPCSKTAQCVNTYGGYRCVC 2397
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
2205-2234 5.61e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 39.50  E-value: 5.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181 2205 PCHEMADCTSTGYNYTCKCKRGYAGNGKEC 2234
Cdd:pfam12947    7 GCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1201-1241 3.16e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1514903181 1201 DIDEClADESPCTANAGCVNSAGSFQCPCASGFEaqGPKCI 1241
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
216-259 3.62e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.23  E-value: 3.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1514903181   216 DIDECsETPGVCSaffGYKGCKNLPGSYTCLCNSGYQsNGQTCE 259
Cdd:smart00179    1 DIDEC-ASGNPCQ---NGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
704-743 4.86e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.86e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   704 DIDECEENVCPKKETQCVNNPGSFDCICKVGYTlNGTECI 743
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
501-534 6.03e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 6.03e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   501 DIDECQLPEkACGTNEQCSNMEGSYACHCKEGFT 534
Cdd:smart00179    1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
2540-2707 2.48e-102

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 324.41  E-value: 2.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2540 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD 2619
Cdd:PTZ00184     2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2620 SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftE 2699
Cdd:PTZ00184    82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYE--------------------E 141

                   ....*...
gi 1514903181 2700 FVQMMTAK 2707
Cdd:PTZ00184   142 FVKMMMSK 149
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2545-2678 4.45e-33

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 125.67  E-value: 4.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2545 EEQIAEFKEAFSLFDKDGDGTITTKELGTVMRslgqnpteAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDsEEEI 2624
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFR--------RLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFA 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2625 REAFRVFDKDGNGYISAAELRHVMTNLGekLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:COG5126     72 RAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFE 123
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2550-2612 2.35e-26

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: 103.78  E-value: 2.35e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMA 2612
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
2621-2678 1.37e-17

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 78.83  E-value: 1.37e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2621 EEEIREAFRVFDKDGNGYISAAELRHVMTNL--GEKLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFE 60
NIDO smart00539
Extracellular domain of unknown function in nidogen (entactin) and hypothetical proteins;
1421-1557 1.54e-16

Extracellular domain of unknown function in nidogen (entactin) and hypothetical proteins;


Pssm-ID: 214712  Cd Length: 152  Bit Score: 79.01  E-value: 1.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1421 VFWDDADlTLGDGKLLYQEYSllnisDIYaekVFNRTAQDVSrfETQRGNPRFTPSWMVKITWDHVlpVSYQKINLSETN 1500
Cdd:smart00539    1 PFWADAD-TEGTGKVYYRETT-----DHA---ILDRATESVR--EGFTDMGGFRAKSVVIVTWENV--AAYGSQSSDGTN 67
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1514903181  1501 TFQCILTTDGLRSFALLRYSDMNW----GPGQRTDHNALIGYTDGKNNFHNEIPK----PPNNLF 1557
Cdd:smart00539   68 TFQAVLATDGSRTYAIFLYPSLGWtsdtTAGGDDGVRARAGFNGGDGTFSYTLPAsgeeNIKNLA 132
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2552-2676 5.18e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 62.01  E-value: 5.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMA------RKMKDTDSEEEIr 2625
Cdd:NF041410    30 KQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPppppppDQAPSTELADDL- 108
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2626 eaFRVFDKDGNGYISAAELRHVMTNLGeklTDEEVDEMIREADIDGDGQVN 2676
Cdd:NF041410   109 --LSALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVS 154
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2552-2644 6.61e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 61.62  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRS----LGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEeeirEA 2627
Cdd:NF041410    66 SELFSDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSS----QL 141
                           90
                   ....*....|....*..
gi 1514903181 2628 FRVFDKDGNGYISAAEL 2644
Cdd:NF041410   142 FSALDSDGDGSVSSDEL 158
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1751-1920 4.17e-09

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 57.77  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1751 VYGSLHFITFDGSEYTFKALGEYVIVRLSTSTGSniFTLQGQTAALVVNGQPKLVPALErlaaFYQGAGKVEwrcaeSGD 1830
Cdd:pfam00094    3 VSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVCLKSVT----VIVGDLEIT-----LQK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1831 GLKVLVNDVVIPVsvgvvHVEEKAFAVRCTSMSRCAVVYAEGLyVVVWRGDaGRLTALVEVPQRFYNRTLGLLGLWNSNR 1910
Cdd:pfam00094   72 GGTVLVNGQKVSL-----PYKSDGGEVEILGSGFVVVDLSPGV-GLQVDGD-GRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144
                          170
                   ....*....|
gi 1514903181 1911 TDDFLLSNGR 1920
Cdd:pfam00094  145 EDDFMTPDGT 154
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
138-173 4.40e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 53.76  E-value: 4.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  138 CQTNNGGCHVNALCTNRDGGRDCSCKSGFSGNGFQC 173
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
97-132 1.84e-08

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.22  E-value: 1.84e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181   97 CTTGLHSCHGKAICSNTLGSYTCSCLNGYFGDGFQC 132
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
2550-2578 2.61e-08

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: 51.61  E-value: 2.61e-08
                            10        20
                    ....*....|....*....|....*....
gi 1514903181  2550 EFKEAFSLFDKDGDGTITTKELGTVMRSL 2578
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
544-583 1.25e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 1.25e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   544 DIDECENQKPCHQNGTCLNLAGSFSCTCKHGFSgNGVTCE 583
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
544-583 3.56e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 3.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  544 DIDECENQKPCHQNGTCLNLAGSFSCTCKHGFSGNgvTCE 583
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR--NCE 38
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
181-210 3.86e-07

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 48.36  E-value: 3.86e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181  181 RPGICHWNATCTNNPGSYVCTCNAGYKGNG 210
Cdd:pfam12947    4 NNGGCHPNATCTNTGGSFTCTCNDGYTGDG 33
NIDO pfam06119
Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found ...
1499-1580 7.24e-07

Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found in nidogen and hypothetical proteins of unknown function.


Pssm-ID: 461833  Cd Length: 90  Bit Score: 49.21  E-value: 7.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1499 TNTFQCILTTDGLRSFALLRYSD--MNW-------GPGQRTDHNALIGYT--DGKNNFHNEipkppnnlfgPGGRY---R 1564
Cdd:pfam06119    1 TNTFQAVLATDGSGSFAIFNYPDggIQWttgkasgGTNGLGGTPAQAGFSagDGDGRYYEL----------PGSGTdsiR 70
                           90
                   ....*....|....*.
gi 1514903181 1565 PQTVTGNTGKLGQLVY 1580
Cdd:pfam06119   71 NLTETSNVGVPGRWVF 86
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
299-338 1.02e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.25  E-value: 1.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  299 DINECDRKNNCDPNAICTNLLGSYQCSCRSGFlgTGTKCT 338
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
299-338 1.07e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 1.07e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   299 DINECDRKNNCDPNAICTNLLGSYQCSCRSGFLgTGTKCT 338
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
951-990 1.13e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 1.13e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   951 DINECSQSGACPKLSTCFNTEGSYHCDCWEGYQyNGIHCE 990
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
549-582 1.41e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 46.82  E-value: 1.41e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  549 ENQKPCHQNGTCLNLAGSFSCTCKHGFSGNGVTC 582
Cdd:pfam12947    3 DNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
1286-1320 1.48e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 46.82  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181 1286 CAKNTT-CHPLARCWNTVGSFTCQCRLGYAGNGTYC 1320
Cdd:pfam12947    1 CSDNNGgCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1242-1275 3.09e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 3.09e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181  1242 DINECLSNRTCRPDQVCINKPGSYQCSCPLGHHE 1275
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTD 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
304-337 3.18e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 45.67  E-value: 3.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  304 DRKNNCDPNAICTNLLGSYQCSCRSGFLGTGTKC 337
Cdd:pfam12947    3 DNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
339-370 3.87e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 3.87e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181   339 DIDECAASNICPSNAVCVNTAGSFFCDCGQGY 370
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
837-868 4.18e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 45.28  E-value: 4.18e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  837 PHNCSLLAMCNNTEGSYICKCMEGYLGDGFTC 868
Cdd:pfam12947    5 NGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1074-1110 4.40e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 4.40e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1514903181  1074 DVDECLNNSACSDNSICVNTEGSFLCLCDDGFSSNGT 1110
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1745-1919 6.60e-06

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 48.55  E-value: 6.60e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1745 APGIGMVYGSLHFITFDGSEYTFKALGEYVIVRLSTSTGSNIFTLQGQtAALVVNGQPKLVpalerlaAFYQGAGKVEwr 1824
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPTFSVLLKNV-PCGGGATCLKSV-------KVELNGDEIE-- 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1825 caESGDGLKVLVNDVVIPVSvgvvHVEEKAFAVRCTSMSRCAVVYAEGLYVVVWrgdAGRLTALVEVPQRFYNRTLGLLG 1904
Cdd:smart00216   78 --LKDDNGKVTVNGQQVSLP----YKTSDGSIQIRSSGGYLVVITSLGLIQVTF---DGLTLLSVQLPSKYRGKTCGLCG 148
                           170
                    ....*....|....*
gi 1514903181  1905 LWNSNRTDDFLLSNG 1919
Cdd:smart00216  149 NFDGEPEDDFRTPDG 163
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
339-370 6.67e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 6.67e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  339 DIDECAASNICPSNAVCVNTAGSFFCDCGQGY 370
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGY 32
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2577-2676 7.84e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 49.68  E-value: 7.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2577 SLGQNPTEAELQ-DMINEVDADGNGTIDFPEFLTMMARKmKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTN----L 2651
Cdd:NF041410    18 SSTSSARSQQFQkQLFAKLDSDGDGSVSQDELSSALSSK-SDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPppppP 96
                           90       100
                   ....*....|....*....|....*
gi 1514903181 2652 GEKLTDEEVDEMIREADIDGDGQVN 2676
Cdd:NF041410    97 DQAPSTELADDLLSALDTDGDGSIS 121
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1242-1274 8.28e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 8.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1242 DINECLSNRTCRPDQVCINKPGSYQCSCPLGHH 1274
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
789-824 1.02e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.51  E-value: 1.02e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  789 CQSQHGGCHPAASCTNSPGSYKCTCPFGMNGSGFDC 824
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
260-298 1.23e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 1.23e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   260 DINECE-INICSSFADCTNLPGSYRCTCPEGFVgNGLACV 298
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
175-208 1.46e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.16  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  175 DDNECARPGICHWNATCTNNPGSYVCTCNAGYKG 208
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1074-1106 2.19e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 2.19e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1074 DVDECLNNSACSDNSICVNTEGSFLCLCDDGFS 1106
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
175-211 2.52e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 2.52e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1514903181   175 DDNECARPGICHWNATCTNNPGSYVCTCNAGYKGNGN 211
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
870-900 2.60e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 2.60e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1514903181   870 DVDECLSPSICRNNMTCQNFPGTYTCTCTVG 900
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
260-292 3.47e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  260 DINECE-INICSSFADCTNLPGSYRCTCPEGFVG 292
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
951-990 3.64e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 3.64e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  951 DINECSQSGACPKLSTCFNTEGSYHCDCWEGYQynGIHCE 990
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
870-909 4.14e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.62  E-value: 4.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  870 DVDECLSPSICRNNMTCQNFPGTYTCTCTVGlvYDLGTCV 909
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPG--YTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1158-1197 5.27e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.27e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181  1158 DIDECSGSNNesiCQPHSTCVNVPGSYKCDCNLGFLLNRT 1197
Cdd:smart00179    1 DIDECASGNP---CQNGGTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
459-492 5.76e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 5.76e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   459 DVNECLvDNGGCRNRAKCVNSMGSFSCTCPSGFQ 492
Cdd:smart00179    1 DIDECA-SGNPCQNGGTCVNTVGSYRCECPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
269-297 6.39e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 42.20  E-value: 6.39e-05
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  269 CSSFADCTNLPGSYRCTCPEGFVGNGLAC 297
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
459-495 6.70e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 6.70e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1514903181  459 DVNECLvDNGGCRNRAKCVNSMGSFSCTCPSGFQLVN 495
Cdd:cd00054      1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
428-454 7.12e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.12e-05
                           10        20
                   ....*....|....*....|....*..
gi 1514903181  428 CHVNALCINVPGKFNCSCMVGYTGDGV 454
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGV 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
592-622 7.41e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.41e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1514903181  592 GMCHLQANCYNYPGEFMCICHQGFNGDGFTC 622
Cdd:pfam12947    6 GGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1282-1321 8.44e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 8.44e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181  1282 DNNECAKNTTCHPLARCWNTVGSFTCQCRLGYAgNGTYCK 1321
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1158-1196 8.91e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.85  E-value: 8.91e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1514903181 1158 DIDECSGSNnesICQPHSTCVNVPGSYKCDCNLGFLLNR 1196
Cdd:cd00054      1 DIDECASGN---PCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1322-1353 9.32e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 9.32e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181  1322 DIDECSTSSLrCHKSSQCINTPGSYICVCAPG 1353
Cdd:smart00179    1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPG 31
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
748-783 1.04e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.43  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  748 CESGVNSCSKFAQCDNTIGSHLCFCLNGFTGDGKNC 783
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
93-133 1.35e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.46  E-value: 1.35e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181    93 DIDECTTGlHSCHGKAICSNTLGSYTCSCLNGYFgDGFQCQ 133
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
418-452 1.39e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  418 DVDECAIEKRCHVNALCINVPGKFNCSCMVGYTGD 452
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1282-1315 1.46e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181 1282 DNNECAKNTTCHPLARCWNTVGSFTCQCRLGYAG 1315
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
93-128 1.50e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.50e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181   93 DIDECTTGlHSCHGKAICSNTLGSYTCSCLNGYFGD 128
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1322-1353 1.51e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.51e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1322 DIDECSTSSLrCHKSSQCINTPGSYICVCAPG 1353
Cdd:cd00054      1 DIDECASGNP-CQNGGTCVNTVGSYRCSCPPG 31
EGF_CA pfam07645
Calcium-binding EGF domain;
1033-1064 1.63e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1033 DVDECATGKAQCPNASNCQNTVGWYFCECWDG 1064
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
339-369 2.19e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.19e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  339 DIDECA-ASNICPSNAVCVNTAGSFFCDCGQG 369
Cdd:pfam07645    1 DVDECAtGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
1074-1104 2.23e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.23e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1074 DVDECLNNSA-CSDNSICVNTEGSFLCLCDDG 1104
Cdd:pfam07645    1 DVDECATGTHnCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
1033-1073 2.42e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 2.42e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1033 DVDECATGkAQCPNASNCQNTVGWYFCECWDGYTGNQTvCE 1073
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTDGRN-CE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1117-1156 3.34e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.34e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1117 DIDECidEFGPLCTNG-TCINTIGSFHCVCDMGFwSNDTRC 1156
Cdd:smart00179    1 DIDEC--ASGNPCQNGgTCVNTVGSYRCECPPGY-TDGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
744-783 3.41e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   744 DVDECESGvNSCSKFAQCDNTIGSHLCFCLNGFTgDGKNC 783
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
379-416 3.51e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.51e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1514903181   379 DVDECAIRH-CSPYSSCENLPGSFICSCIAGFEgDGLIC 416
Cdd:smart00179    1 DIDECASGNpCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
826-869 4.58e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.92  E-value: 4.58e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1514903181   826 DVDECNEnstlPHNCSLLAMCNNTEGSYICKCMEGYLgDGFTCE 869
Cdd:smart00179    1 DIDECAS----GNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
991-1019 4.85e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.85e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  991 DINECSVGNFICPDNSTCYNKEGGYNCPC 1019
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA pfam07645
Calcium-binding EGF domain;
2369-2397 4.94e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.94e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181 2369 DLDECKTNEAPCSKTAQCVNTYGGYRCVC 2397
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
2205-2234 5.61e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 39.50  E-value: 5.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181 2205 PCHEMADCTSTGYNYTCKCKRGYAGNGKEC 2234
Cdd:pfam12947    7 GCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
785-816 5.74e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.54  E-value: 5.74e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181   785 DINECQSQHGgCHPAASCTNSPGSYKCTCPFG 816
Cdd:smart00179    1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPG 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
785-816 6.81e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 6.81e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  785 DINECQSQHGgCHPAASCTNSPGSYKCTCPFG 816
Cdd:cd00054      1 DIDECASGNP-CQNGGTCVNTVGSYRCSCPPG 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
379-412 7.97e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 7.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  379 DVDECAIRH-CSPYSSCENLPGSFICSCIAGFEGD 412
Cdd:cd00054      1 DIDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
418-450 8.51e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 8.51e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1514903181   418 DVDECAIEKRCHVNALCINVPGKFNCSCMVGYT 450
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1117-1149 9.71e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 9.71e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1117 DIDECiDEFGPLCTNGTCINTIGSFHCVCDMGF 1149
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
584-623 1.54e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 1.54e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   584 DINECAIEGMCHLQANCYNYPGEFMCICHQGFNgDGFTCT 623
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
584-618 1.84e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 1.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  584 DINECAIEGMCHLQANCYNYPGEFMCICHQGFNGD 618
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA pfam07645
Calcium-binding EGF domain;
1322-1353 2.00e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.99  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1322 DIDECSTSSLRCHKSSQCINTPGSYICVCAPG 1353
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
744-783 2.52e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 2.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  744 DVDECESGvNSCSKFAQCDNTIGSHLCFCLNGFTgdGKNC 783
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNC 37
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
463-492 2.65e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 37.58  E-value: 2.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181  463 CLVDNGGCRNRAKCVNSMGSFSCTCPSGFQ 492
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYT 30
EGF_CA pfam07645
Calcium-binding EGF domain;
870-900 2.87e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.22  E-value: 2.87e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  870 DVDECLSPS-ICRNNMTCQNFPGTYTCTCTVG 900
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
1117-1148 2.96e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.22  E-value: 2.96e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1117 DIDECIDEFGPLCTNGTCINTIGSFHCVCDMG 1148
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1201-1241 3.16e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1514903181 1201 DIDEClADESPCTANAGCVNSAGSFQCPCASGFEaqGPKCI 1241
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
216-259 3.62e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.23  E-value: 3.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1514903181   216 DIDECsETPGVCSaffGYKGCKNLPGSYTCLCNSGYQsNGQTCE 259
Cdd:smart00179    1 DIDEC-ASGNPCQ---NGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1033-1067 3.74e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181 1033 DVDECATGkAQCPNASNCQNTVGWYFCECWDGYTG 1067
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
826-869 3.93e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1514903181  826 DVDECnensTLPHNCSLLAMCNNTEGSYICKCMEGYLGDgfTCE 869
Cdd:cd00054      1 DIDEC----ASGNPCQNGGTCVNTVGSYRCSCPPGYTGR--NCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1201-1241 4.58e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.58e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1201 DIDEClADESPCTANAGCVNSAGSFQCPCASGFEaQGPKCI 1241
Cdd:smart00179    1 DIDEC-ASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
704-743 4.86e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.86e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   704 DIDECEENVCPKKETQCVNNPGSFDCICKVGYTlNGTECI 743
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
501-534 6.03e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 6.03e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   501 DIDECQLPEkACGTNEQCSNMEGSYACHCKEGFT 534
Cdd:smart00179    1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA pfam07645
Calcium-binding EGF domain;
704-734 6.76e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.45  E-value: 6.76e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181  704 DIDECEE--NVCPKKETqCVNNPGSFDCICKVG 734
Cdd:pfam07645    1 DVDECATgtHNCPANTV-CVNTIGSFECRCPDG 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
388-416 8.48e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 36.04  E-value: 8.48e-03
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  388 CSPYSSCENLPGSFICSCIAGFEGDGLIC 416
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
2540-2707 2.48e-102

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 324.41  E-value: 2.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2540 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD 2619
Cdd:PTZ00184     2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2620 SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftE 2699
Cdd:PTZ00184    82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYE--------------------E 141

                   ....*...
gi 1514903181 2700 FVQMMTAK 2707
Cdd:PTZ00184   142 FVKMMMSK 149
PTZ00183 PTZ00183
centrin; Provisional
2538-2694 3.10e-52

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 181.43  E-value: 3.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2538 NEADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKD 2617
Cdd:PTZ00183     6 SERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGE 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2618 TDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRnlviIQKRTNPF 2694
Cdd:PTZ00183    86 RDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYR----IMKKTNLF 158
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2545-2678 4.45e-33

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 125.67  E-value: 4.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2545 EEQIAEFKEAFSLFDKDGDGTITTKELGTVMRslgqnpteAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDsEEEI 2624
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFR--------RLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFA 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2625 REAFRVFDKDGNGYISAAELRHVMTNLGekLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:COG5126     72 RAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFE 123
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2550-2612 2.35e-26

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: 103.78  E-value: 2.35e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMA 2612
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2623-2705 4.36e-24

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: 97.23  E-value: 4.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2623 EIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftEFVQ 2702
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFE--------------------EFLE 60

                   ...
gi 1514903181 2703 MMT 2705
Cdd:cd00051     61 LMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2530-2649 2.89e-20

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 89.08  E-value: 2.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRNRGLNEADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLT 2609
Cdd:COG5126     14 LDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRR 93
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1514903181 2610 MMARKmkdTDSEEEIREAFRVFDKDGNGYISAAELRHVMT 2649
Cdd:COG5126     94 LLTAL---GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
2550-2697 7.50e-19

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: 86.04  E-value: 7.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAE-LQDMINEVDADGNGTIDFPEFltmmarkmKDTDSE-EEIREA 2627
Cdd:cd16180      1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIEtVRLMINMFDRDRSGTINFDEF--------VGLWKYiQDWRRL 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2628 FRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKRTNPFSVF 2697
Cdd:cd16180     73 FRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKRLTDAFRKY 142
EF-hand_7 pfam13499
EF-hand domain pair;
2621-2678 1.37e-17

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 78.83  E-value: 1.37e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2621 EEEIREAFRVFDKDGNGYISAAELRHVMTNL--GEKLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFE 60
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
2551-2677 1.33e-16

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: 82.02  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSL-----GQNPTEAELQDMINEV----DADGNGTIDFPEFLTMMA--------- 2612
Cdd:cd15902      1 FMEVWMHFDADGNGYIEGKELDSFLRELlkalnGKDKTDDEVAEKKKEFmekyDENEDGKIEIRELANILPteenflllf 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2613 RKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKL--------TDEEVDEMIREADIDGDGQVNY 2677
Cdd:cd15902     81 RREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNkkhvsppkLDEYTKLILKEFDANKDGKLEL 153
NIDO smart00539
Extracellular domain of unknown function in nidogen (entactin) and hypothetical proteins;
1421-1557 1.54e-16

Extracellular domain of unknown function in nidogen (entactin) and hypothetical proteins;


Pssm-ID: 214712  Cd Length: 152  Bit Score: 79.01  E-value: 1.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1421 VFWDDADlTLGDGKLLYQEYSllnisDIYaekVFNRTAQDVSrfETQRGNPRFTPSWMVKITWDHVlpVSYQKINLSETN 1500
Cdd:smart00539    1 PFWADAD-TEGTGKVYYRETT-----DHA---ILDRATESVR--EGFTDMGGFRAKSVVIVTWENV--AAYGSQSSDGTN 67
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1514903181  1501 TFQCILTTDGLRSFALLRYSDMNW----GPGQRTDHNALIGYTDGKNNFHNEIPK----PPNNLF 1557
Cdd:smart00539   68 TFQAVLATDGSRTYAIFLYPSLGWtsdtTAGGDDGVRARAGFNGGDGTFSYTLPAsgeeNIKNLA 132
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
2551-2679 2.29e-15

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: 75.01  E-value: 2.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMkdtdSEEEIREAFRV 2630
Cdd:cd15898      2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT----ERPELEPIFKK 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2631 FDKDGNGYISAAELRHVMTN-LGEKLTDEEVDEMIREADIDG-DGQVNYEG 2679
Cdd:cd15898     78 YAGTNRDYMTLEEFIRFLREeQGENVSEEECEELIEKYEPEReNRQLSFEG 128
EF-hand_7 pfam13499
EF-hand domain pair;
2552-2611 2.47e-15

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 72.67  E-value: 2.47e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSL--GQNPTEAELQDMINEVDADGNGTIDFPEFLTMM 2611
Cdd:pfam13499    5 KEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
2600-2678 2.03e-14

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: 71.41  E-value: 2.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2600 GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK-----LTDEEVDEMIREADIDGDGQ 2674
Cdd:cd16252     15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAADTDGDGR 94

                   ....
gi 1514903181 2675 VNYE 2678
Cdd:cd16252     95 IDFQ 98
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
2517-2678 1.54e-13

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 73.24  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2517 PQELGTLGW--YSVCF------DHRNRGLNEADQLTEEQI-AEFKEAFSLFDKDGDGTITTKELgTVMRSLGQNP--TEA 2585
Cdd:cd15899     82 PDEDGHVSWdeYKNDTygsvgdDEENVADNIKEDEEYKKLlLKDKKRFEAADQDGDLILTLEEF-LAFLHPEESPymLDF 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2586 ELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI---REAFR-VFDKDGNGYISAAELRHVMTNLGEKLTDEEVD 2661
Cdd:cd15899    161 VIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVkveKERFVeLRDKDKDGKLDGEELLSWVDPSNQEIALEEAK 240
                          170
                   ....*....|....*..
gi 1514903181 2662 EMIREADIDGDGQVNYE 2678
Cdd:cd15899    241 HLIAESDENKDGKLSPE 257
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
2538-2678 2.04e-13

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: 72.73  E-value: 2.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2538 NEADQLTEEQ--IAEFKEAFSLFDKDGDGTITTKELgtvmrSLGQNPTE------AELQDMINEVDADGNGTIDFPEFLT 2609
Cdd:cd16227    109 MIKDSTEDDLklLEDDKEMFEAADLNKDGKLDKTEF-----SAFQHPEEyphmhpVLIEQTLRDKDKDNDGFISFQEFLG 183
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1514903181 2610 MMArkmKDTDSEEEIREAFRV---FDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:cd16227    184 DRA---GHEDKEWLLVEKDRFdedYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFD 252
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
2549-2678 1.11e-12

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: 70.46  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2549 AEFKEAFSLFDKDGDGTITTKELGTVMRSL--GQNPT--EAELQDMIN----EVDADGNGTIDFPEFLTMMARK----MK 2616
Cdd:cd15902     90 VEFMKIWRKYDTDGSGFIEAKELKGFLKDLllKNKKHvsPPKLDEYTKlilkEFDANKDGKLELDEMAKLLPVQenflLK 169
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1514903181 2617 DTDS------EEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK------LTDEE--VDEMIREADIDGDGQVNYE 2678
Cdd:cd15902    170 FQILgamdltKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKnkadidKPDLEnfRDAILRACDKNKDGKIQKT 245
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
2600-2678 1.24e-12

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: 66.02  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2600 GTIDFPEFLTMMARKMKdtdSEEEIREAFRVFDKDGNGYISAAELRHVMTNL---GEKLTDEEVDEMIREADIDGDGQVN 2676
Cdd:cd16251     15 GSFNYKKFFEHVGLKQK---SEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLAAGDTDGDGKIG 91

                   ..
gi 1514903181 2677 YE 2678
Cdd:cd16251     92 VE 93
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
2555-2697 1.70e-12

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 67.66  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2555 FSLFDKDGDGTITTKELGTVMrSLGQ----NPTEAELqdMINEVDADGNGTIDFPEFLTMMarkmkdtDSEEEIREAFRV 2630
Cdd:cd16183      6 FQRVDKDRSGQISATELQQAL-SNGTwtpfNPETVRL--MIGMFDRDNSGTINFQEFAALW-------KYITDWQNCFRS 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2631 FDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKRTNPFSVF 2697
Cdd:cd16183     76 FDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFIQCCVVLQTLTDSFRRY 142
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
2550-2697 4.50e-11

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: 63.77  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKdtdseeeIREAFR 2629
Cdd:cd16185      1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAALHQFLSN-------MQNGFE 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1514903181 2630 VFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKRTNPFSVF 2697
Cdd:cd16185     74 QRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIELCIFLASARNLFQAF 141
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
2517-2678 2.39e-10

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: 63.76  E-value: 2.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2517 PQELGTLGWYsvcfDHRNR--GLNEADQLTEEQIAEFKEA-------FSLFDKDGDGTITTKELGTVMrslgqNPTEAE- 2586
Cdd:cd16226     82 PNKDGKLSWE----EYKKAtyGFLDDEEEDDDLHESYKKMirrderrWKAADQDGDGKLTKEEFTAFL-----HPEEFPh 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2587 -----LQDMINEVDADGNGTIDFPEFLTMMARK---MKDTDSEEEIREAFRVF-DKDGNGYISAAELRHVMTNLGEKLTD 2657
Cdd:cd16226    153 mrdivVQETLEDIDKNKDGFISLEEYIGDMYRDddeEEDPDWVKSEREQFKEFrDKNKDGKMDREEVKDWILPEDYDHAE 232
                          170       180
                   ....*....|....*....|.
gi 1514903181 2658 EEVDEMIREADIDGDGQVNYE 2678
Cdd:cd16226    233 AEAKHLIYEADDDKDGKLTKE 253
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
2550-2697 4.33e-10

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: 60.91  E-value: 4.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2550 EFKEAFSLFDKDgDGTITTKELGTVMRSLGQNPTE-----AELQDMINEVDADGNGTIDFPEFlTMMARKMKDtdseeeI 2624
Cdd:cd15897      1 QLRNVFQAVAGD-DGEISATELQQALSNVGWTHFDlgfslETCRSMIAMMDRDHSGKLNFSEF-KGLWNYIKA------W 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2625 REAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADiDGDGQVNYEGHVRNLVIIQKRTNPFSVF 2697
Cdd:cd15897     73 QEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYD-RGRGNIDFDDFIQCCVRLQRLTDAFRRY 144
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2552-2676 5.18e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 62.01  E-value: 5.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMA------RKMKDTDSEEEIr 2625
Cdd:NF041410    30 KQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPppppppDQAPSTELADDL- 108
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2626 eaFRVFDKDGNGYISAAELRHVMTNLGeklTDEEVDEMIREADIDGDGQVN 2676
Cdd:NF041410   109 --LSALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVS 154
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2552-2644 6.61e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 61.62  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRS----LGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEeeirEA 2627
Cdd:NF041410    66 SELFSDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSS----QL 141
                           90
                   ....*....|....*..
gi 1514903181 2628 FRVFDKDGNGYISAAEL 2644
Cdd:NF041410   142 FSALDSDGDGSVSSDEL 158
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1751-1920 4.17e-09

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 57.77  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1751 VYGSLHFITFDGSEYTFKALGEYVIVRLSTSTGSniFTLQGQTAALVVNGQPKLVPALErlaaFYQGAGKVEwrcaeSGD 1830
Cdd:pfam00094    3 VSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVCLKSVT----VIVGDLEIT-----LQK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1831 GLKVLVNDVVIPVsvgvvHVEEKAFAVRCTSMSRCAVVYAEGLyVVVWRGDaGRLTALVEVPQRFYNRTLGLLGLWNSNR 1910
Cdd:pfam00094   72 GGTVLVNGQKVSL-----PYKSDGGEVEILGSGFVVVDLSPGV-GLQVDGD-GRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144
                          170
                   ....*....|
gi 1514903181 1911 TDDFLLSNGR 1920
Cdd:pfam00094  145 EDDFMTPDGT 154
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
138-173 4.40e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 53.76  E-value: 4.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  138 CQTNNGGCHVNALCTNRDGGRDCSCKSGFSGNGFQC 173
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
2551-2692 5.06e-09

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


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 59.72  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSLGQ------NPTEAELQDM----INEVDADGNGTIDFPEFLTMMA-------- 2612
Cdd:cd16178      1 FAEIWQHFDADESGYIEGKELDNFFKDLLKklgtkdTISADEVQDVkecfMSAYDVTGDGRIQIQELANIILpddenfll 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2613 --RKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL----GEKLTDEEVDE----MIREADIDGDGQVNYEGHVR 2682
Cdd:cd16178     81 ffRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLflqhKKVITEDKLDEytdtMMKIFDKNKDGRLDLNDMAR 160
                          170
                   ....*....|
gi 1514903181 2683 nLVIIQKRTN 2692
Cdd:cd16178    161 -ILALQENFL 169
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
2551-2619 6.75e-09

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 54.28  E-value: 6.75e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINevdadgngTIDFPEFLTMMARKMKDTD 2619
Cdd:cd22949      5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDALPA--------SMNWDQFENWAKKKLAYSD 65
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
97-132 1.84e-08

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.22  E-value: 1.84e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181   97 CTTGLHSCHGKAICSNTLGSYTCSCLNGYFGDGFQC 132
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EF-hand_6 pfam13405
EF-hand domain;
2623-2652 2.53e-08

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 51.79  E-value: 2.53e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181 2623 EIREAFRVFDKDGNGYISAAELRHVMTNLG 2652
Cdd:pfam13405    1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
2550-2578 2.61e-08

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: 51.61  E-value: 2.61e-08
                            10        20
                    ....*....|....*....|....*....
gi 1514903181  2550 EFKEAFSLFDKDGDGTITTKELGTVMRSL 2578
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
2548-2639 2.93e-08

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: 55.61  E-value: 2.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2548 IAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDseeeireA 2627
Cdd:cd16180     66 IQDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKRLTD-------A 138
                           90
                   ....*....|..
gi 1514903181 2628 FRVFDKDGNGYI 2639
Cdd:cd16180    139 FRKYDTNRTGYA 150
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
2600-2675 3.58e-08

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: 53.29  E-value: 3.58e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2600 GTIDFPEFLTMMARKMKdtdSEEEIREAFRVFDKDGNGYISAAELRHVMTNL---GEKLTDEEVDEMIREADIDGDGQV 2675
Cdd:cd16254     15 DSFDYKKFFEMVGLKKK---SADDVKKVFHILDKDKSGFIEEDELKFVLKGFspdGRDLSDKETKALLAAGDKDGDGKI 90
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
2623-2651 4.26e-08

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: 50.84  E-value: 4.26e-08
                            10        20
                    ....*....|....*....|....*....
gi 1514903181  2623 EIREAFRVFDKDGNGYISAAELRHVMTNL 2651
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_8 pfam13833
EF-hand domain pair;
2562-2613 5.97e-08

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 51.16  E-value: 5.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2562 GDGTITTKELGTVMRSLG-QNPTEAELQDMINEVDADGNGTIDFPEFLTMMAR 2613
Cdd:pfam13833    1 EKGVITREELKRALALLGlKDLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
EF-hand_8 pfam13833
EF-hand domain pair;
2635-2678 6.72e-08

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 51.16  E-value: 6.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1514903181 2635 GNGYISAAELRHVMTNLGEK-LTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:pfam13833    1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFD 45
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
2556-2681 9.62e-08

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: 54.15  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2556 SLFDK--DGDGTITTKELGTVMRSL--------GQNPTEAELQdMINEVDADGNGTIDFPEFLTMMARKmkdtdseEEIR 2625
Cdd:cd16182      4 ELFEKlaGEDEEIDAVELQKLLNASllkdmpkfDGFSLETCRS-LIALMDTNGSGRLDLEEFKTLWSDL-------KKWQ 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1514903181 2626 EAFRVFDKDGNGYISAAELRHVMTNLGEKLtDEEVDEMIREADIDGDGQVNYEGHV 2681
Cdd:cd16182     76 AIFKKFDTDRSGTLSSYELRKALESAGFHL-SNKVLQALVLRYADSTGRITFEDFV 130
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
2530-2678 1.02e-07

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: 55.79  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHR-----NRGLNEADQLT-EEQIAEFKEAFSLFDKDGDGTITTKELGT-VMRSLgQNPTEAELQDMINEVDADGNGTI 2602
Cdd:cd16227     11 FDHEavlgsRKEAEEFDELPpEEAKRRLAVLAKKMDLNDDGFIDRKELKAwILRSF-KMLDEEEANERFEEADEDGDGKV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2603 DFPEFLT----MMARKM----KDTDSEEEI-----REAFRVFDKDGNGYISAAELrHVMTNLGE--KLTDEEVDEMIREA 2667
Cdd:cd16227     90 TWEEYLAdsfgYDDEDNeemiKDSTEDDLKlleddKEMFEAADLNKDGKLDKTEF-SAFQHPEEypHMHPVLIEQTLRDK 168
                          170
                   ....*....|.
gi 1514903181 2668 DIDGDGQVNYE 2678
Cdd:cd16227    169 DKDNDGFISFQ 179
EGF_CA smart00179
Calcium-binding EGF-like domain;
544-583 1.25e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 1.25e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   544 DIDECENQKPCHQNGTCLNLAGSFSCTCKHGFSgNGVTCE 583
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
2551-2674 1.33e-07

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 55.49  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSL--GQNPT--------EAELQDMINEV----DADGNGTIDFPE---------- 2606
Cdd:cd16179      1 FMDVWNHYDTDGNGYIEGTELDGFLREFvsSVNPEdvgpevvsETALEELKEEFmeayDENQDGRIDIRElaqllpteen 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2607 FLTMMARKMKdTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL-----------GEKLTdEEVDEMIREADIDGDGQ 2674
Cdd:cd16179     81 FLLLFRRDNP-LDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLlkeakrdndvsEDKLI-EYTDTILQLFDRNKDGK 157
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
2623-2651 1.47e-07

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: 49.32  E-value: 1.47e-07
                           10        20
                   ....*....|....*....|....*....
gi 1514903181 2623 EIREAFRVFDKDGNGYISAAELRHVMTNL 2651
Cdd:pfam00036    1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
2543-2674 1.58e-07

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 55.13  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2543 LTEEQIA-------------EFKEAFSLFDKDGDGTITTKELGTVM---------------------RSL---------- 2578
Cdd:cd16224     53 LTEEELSswiqqsfrhyaleDAKQQFPEYDKDGDGAVTWDEYNMQMydrvidydedtvlddeeeesfRQLhlkdkkrfdk 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2579 -------GQNPTE-------AE--------LQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEE-EIREAFRV---FD 2632
Cdd:cd16224    133 antdggpGLNLTEfiafehpEEvdymtefvIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEwIIVEKDRFvndYD 212
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1514903181 2633 KDGNGYISAAE-LRHVMTNlGEKLTDEEVDEMIREADIDGDGQ 2674
Cdd:cd16224    213 KDNDGKLDPQElLPWVVPN-NYGIAQEEALHLIDEMDLNGDGR 254
EF-hand_6 pfam13405
EF-hand domain;
2550-2579 1.74e-07

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 49.10  E-value: 1.74e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLG 2579
Cdd:pfam13405    1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
2551-2675 1.96e-07

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: 54.84  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEA------ELQDMINEVDADGNGTIDFPE----------FLTMMARK 2614
Cdd:cd16176      1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAglelsdQMKAFVDQYGQSTDGKIGIVElaqilpteenFLLFFRQQ 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2615 MKdtdSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLT--------DEEVDEMIREADIDGDGQV 2675
Cdd:cd16176     81 LK---SSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANkpfdesklEEYTHTMLKMFDSNNDGKL 146
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
2549-2654 2.88e-07

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: 54.07  E-value: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2549 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ--------NPTEAELQDMINEVDADGNGTIDfpefLTMMARKMKDTD- 2619
Cdd:cd16176     85 EEFMQTWRKYDADHSGFIEADELKSFLKDLLKkankpfdeSKLEEYTHTMLKMFDSNNDGKLG----LTEMARLLPVQEn 160
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1514903181 2620 ----------SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK 2654
Cdd:cd16176    161 fllkfqgvkmCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEK 205
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
2550-2578 3.21e-07

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: 48.55  E-value: 3.21e-07
                           10        20
                   ....*....|....*....|....*....
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSL 2578
Cdd:pfam00036    1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
544-583 3.56e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 3.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  544 DIDECENQKPCHQNGTCLNLAGSFSCTCKHGFSGNgvTCE 583
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR--NCE 38
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
2555-2703 3.72e-07

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: 52.27  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2555 FSLFDKDGDGTITTKEL-GTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFltmmarkmkdtdSE-----EEIREAF 2628
Cdd:cd16184      6 FQAVDRDRSGKISAKELqQALVNGNWSHFNDETCRLMIGMFDKDKSGTIDIYEF------------QAlwnyiQQWKQVF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2629 RVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKRTNPFSV------------ 2696
Cdd:cd16184     74 QQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRARRSLTLDQFIQVCVQLQSLTDAFRQrdtqmtgtitis 153

                   ....*..
gi 1514903181 2697 FTEFVQM 2703
Cdd:cd16184    154 YEDFLTM 160
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
181-210 3.86e-07

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 48.36  E-value: 3.86e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181  181 RPGICHWNATCTNNPGSYVCTCNAGYKGNG 210
Cdd:pfam12947    4 NNGGCHPNATCTNTGGSFTCTCNDGYTGDG 33
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
2586-2614 3.93e-07

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: 48.14  E-value: 3.93e-07
                            10        20
                    ....*....|....*....|....*....
gi 1514903181  2586 ELQDMINEVDADGNGTIDFPEFLTMMARK 2614
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
2542-2610 5.26e-07

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: 50.22  E-value: 5.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2542 QLTEEQIAEFKEAFSLFDKDGDGTITTKE----LGTVMRSLGQNP-TEAELQDMINEVDADGNGTIDFPEFLTM 2610
Cdd:cd16252     30 QTSEQQEEAIRKAFQMLDKDKSGFIEWNEikyiLSTVPSSMPVAPlSDEEAEAMIQAADTDGDGRIDFQEFSDM 103
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
2600-2678 5.78e-07

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: 50.11  E-value: 5.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2600 GTIDFPEFLTM--MARKmkdtdSEEEIREAFRVFDKDGNGYISAAELRHVMTNL---GEKLTDEEVDEMIREADIDGDGQ 2674
Cdd:cd16255     15 DSFNFKKFFATsgLSKK-----SADDVKKVFEIIDQDKSGFIEEEELKLFLQNFssgARELTDAETKAFLKAGDSDGDGK 89

                   ....
gi 1514903181 2675 VNYE 2678
Cdd:cd16255     90 IGVE 93
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
2552-2649 6.03e-07

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: 51.07  E-value: 6.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLT----MMARkmkdtdseEEIREA 2627
Cdd:cd16202      3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQfynrLTKR--------PEIEEL 74
                           90       100
                   ....*....|....*....|..
gi 1514903181 2628 FRVFDKDGnGYISAAELRHVMT 2649
Cdd:cd16202     75 FKKYSGDD-EALTVEELRRFLQ 95
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
2551-2704 6.16e-07

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 51.46  E-value: 6.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMR------SLGQNPTEAELQDMINEVD----------ADGNGTIDFPEFLTMMARK 2614
Cdd:cd15900      2 FEIAFKMFDLDGDGELDKEEFNKVQSiirsqtSVGQRHRDHTNGESTKLGMnstlaryffgKDGKQKLSIEKFLEFQENL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2615 MKDTDseeEIREAFRvFDKDGNGYISAAELRHVM-TNLGEKLTDEEVDEMIREADIDGDGQVNYEghvrnlviiqkrtnp 2693
Cdd:cd15900     82 QEEID---DVDTALT-FYHLAGASIDRKTFKRAAkVVAGVELSDHVVDVVFTIFDEDGDGILSHK--------------- 142
                          170
                   ....*....|.
gi 1514903181 2694 fsvftEFVQMM 2704
Cdd:cd15900    143 -----EFISVM 148
NIDO pfam06119
Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found ...
1499-1580 7.24e-07

Nidogen-like; This is a nidogen-like domain (NIDO) domain and is an extracellular domain found in nidogen and hypothetical proteins of unknown function.


Pssm-ID: 461833  Cd Length: 90  Bit Score: 49.21  E-value: 7.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 1499 TNTFQCILTTDGLRSFALLRYSD--MNW-------GPGQRTDHNALIGYT--DGKNNFHNEipkppnnlfgPGGRY---R 1564
Cdd:pfam06119    1 TNTFQAVLATDGSGSFAIFNYPDggIQWttgkasgGTNGLGGTPAQAGFSagDGDGRYYEL----------PGSGTdsiR 70
                           90
                   ....*....|....*.
gi 1514903181 1565 PQTVTGNTGKLGQLVY 1580
Cdd:pfam06119   71 NLTETSNVGVPGRWVF 86
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
2551-2675 8.07e-07

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


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 52.95  E-value: 8.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSL-------GQNPTEAELQDMINEV----DADGNGTIDFPEFLTMMARK----- 2614
Cdd:cd16177      1 FLEIWKHFDADGNGYIEGKELENFFRELerarrgaGVDSKSANFGEKMKEFmqkyDKNADGRIEMAELAQILPTEenfll 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2615 --MKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL--------GEKLTDEEVDEMIREADIDGDGQV 2675
Cdd:cd16177     81 cfRQHVGSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLlkkanrpyDEKKLQEYTQTILRMFDLNGDGKL 151
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
299-338 1.02e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.25  E-value: 1.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  299 DINECDRKNNCDPNAICTNLLGSYQCSCRSGFlgTGTKCT 338
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
299-338 1.07e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 1.07e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   299 DINECDRKNNCDPNAICTNLLGSYQCSCRSGFLgTGTKCT 338
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
951-990 1.13e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 1.13e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   951 DINECSQSGACPKLSTCFNTEGSYHCDCWEGYQyNGIHCE 990
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
549-582 1.41e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 46.82  E-value: 1.41e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  549 ENQKPCHQNGTCLNLAGSFSCTCKHGFSGNGVTC 582
Cdd:pfam12947    3 DNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
2549-2637 1.41e-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: 49.97  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2549 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPteaELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAF 2628
Cdd:cd15898     36 KELKKLFKEVDTNGDGTLTFDEFEELYKSLTERP---ELEPIFKKYAGTNRDYMTLEEFIRFLREEQGENVSEEECEELI 112

                   ....*....
gi 1514903181 2629 RVFDKDGNG 2637
Cdd:cd15898    113 EKYEPEREN 121
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
1286-1320 1.48e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 46.82  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181 1286 CAKNTT-CHPLARCWNTVGSFTCQCRLGYAGNGTYC 1320
Cdd:pfam12947    1 CSDNNGgCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
2542-2612 1.50e-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: 48.68  E-value: 1.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2542 QLTEEQIaefKEAFSLFDKDGDGTITTKELGTVMRSL---GQNPTEAELQDMINEVDADGNGTIDFPEFLTMMA 2612
Cdd:cd16251     30 QKSEDQI---KKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLAAGDTDGDGKIGVEEFATLVA 100
EGF_CA pfam07645
Calcium-binding EGF domain;
93-124 2.20e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 46.08  E-value: 2.20e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181   93 DIDECTTGLHSCHGKAICSNTLGSYTCSCLNG 124
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
2548-2639 2.75e-06

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: 49.74  E-value: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2548 IAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEaELQDMINEVDADGNGTIDFPEFLTMMARKmkdtdseEEIREA 2627
Cdd:cd15897     69 IKAWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSE-QTYDIIIRRYDRGRGNIDFDDFIQCCVRL-------QRLTDA 140
                           90
                   ....*....|..
gi 1514903181 2628 FRVFDKDGNGYI 2639
Cdd:cd15897    141 FRRYDKDQDGQI 152
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
2563-2665 3.06e-06

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 49.68  E-value: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2563 DGTITTKELGTVMRSLG--QNPTEAELQD---MINEVDADGNGTIDFPEFLTMMArkmkdtdSEEEIREAFRVFDKDGNG 2637
Cdd:cd16181     13 DGQIDADELQRCLTQSGisGNYQPFSLETcrlMIAMLDRDHSGKMGFNEFKELWA-------ALNQWKTTFMQYDRDRSG 85
                           90       100
                   ....*....|....*....|....*...
gi 1514903181 2638 YISAAELRHVMTNLGEKLTDEEVDEMIR 2665
Cdd:cd16181     86 TVEPQELQQAIRSFGYNLSPQALNVIVK 113
EGF_CA smart00179
Calcium-binding EGF-like domain;
1242-1275 3.09e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 3.09e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181  1242 DINECLSNRTCRPDQVCINKPGSYQCSCPLGHHE 1275
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTD 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
304-337 3.18e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 45.67  E-value: 3.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  304 DRKNNCDPNAICTNLLGSYQCSCRSGFLGTGTKC 337
Cdd:pfam12947    3 DNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
2620-2663 3.46e-06

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 46.57  E-value: 3.46e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1514903181 2620 SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM 2663
Cdd:cd22949      1 MEEKFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDAL 44
EGF_CA smart00179
Calcium-binding EGF-like domain;
339-370 3.87e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 3.87e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181   339 DIDECAASNICPSNAVCVNTAGSFFCDCGQGY 370
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
837-868 4.18e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 45.28  E-value: 4.18e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  837 PHNCSLLAMCNNTEGSYICKCMEGYLGDGFTC 868
Cdd:pfam12947    5 NGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1074-1110 4.40e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 4.40e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1514903181  1074 DVDECLNNSACSDNSICVNTEGSFLCLCDDGFSSNGT 1110
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
2586-2613 6.30e-06

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: 44.70  E-value: 6.30e-06
                           10        20
                   ....*....|....*....|....*...
gi 1514903181 2586 ELQDMINEVDADGNGTIDFPEFLTMMAR 2613
Cdd:pfam00036    1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
2530-2678 6.41e-06

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: 50.27  E-value: 6.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRN-RGLNEA---DQLTEEQIAE-FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDF 2604
Cdd:cd16226     11 YDHEAfLGKEEAkefDQLTPEESKErLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSW 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2605 PEFLTMMARKMKDTDSEEEIREA-----------FRVFDKDGNGYISAAELRHVmtnlgekLTDEEVDEM----IREA-- 2667
Cdd:cd16226     91 EEYKKATYGFLDDEEEDDDLHESykkmirrderrWKAADQDGDGKLTKEEFTAF-------LHPEEFPHMrdivVQETle 163
                          170
                   ....*....|...
gi 1514903181 2668 DID--GDGQVNYE 2678
Cdd:cd16226    164 DIDknKDGFISLE 176
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1745-1919 6.60e-06

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 48.55  E-value: 6.60e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1745 APGIGMVYGSLHFITFDGSEYTFKALGEYVIVRLSTSTGSNIFTLQGQtAALVVNGQPKLVpalerlaAFYQGAGKVEwr 1824
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPTFSVLLKNV-PCGGGATCLKSV-------KVELNGDEIE-- 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181  1825 caESGDGLKVLVNDVVIPVSvgvvHVEEKAFAVRCTSMSRCAVVYAEGLYVVVWrgdAGRLTALVEVPQRFYNRTLGLLG 1904
Cdd:smart00216   78 --LKDDNGKVTVNGQQVSLP----YKTSDGSIQIRSSGGYLVVITSLGLIQVTF---DGLTLLSVQLPSKYRGKTCGLCG 148
                           170
                    ....*....|....*
gi 1514903181  1905 LWNSNRTDDFLLSNG 1919
Cdd:smart00216  149 NFDGEPEDDFRTPDG 163
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
339-370 6.67e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 6.67e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  339 DIDECAASNICPSNAVCVNTAGSFFCDCGQGY 370
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGY 32
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2577-2676 7.84e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 49.68  E-value: 7.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2577 SLGQNPTEAELQ-DMINEVDADGNGTIDFPEFLTMMARKmKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTN----L 2651
Cdd:NF041410    18 SSTSSARSQQFQkQLFAKLDSDGDGSVSQDELSSALSSK-SDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPppppP 96
                           90       100
                   ....*....|....*....|....*
gi 1514903181 2652 GEKLTDEEVDEMIREADIDGDGQVN 2676
Cdd:NF041410    97 DQAPSTELADDLLSALDTDGDGSIS 121
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1242-1274 8.28e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 8.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1242 DINECLSNRTCRPDQVCINKPGSYQCSCPLGHH 1274
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
2550-2676 9.72e-06

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 49.72  E-value: 9.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2550 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQN------PTEAELQD----MINEVDADGNGTIDFPEfltmMARKMKDTD 2619
Cdd:cd16179     96 EFMKVWREYDKDNSGYIEADELKNFLKHLLKEakrdndVSEDKLIEytdtILQLFDRNKDGKLQLSE----MARLLPVKE 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2620 --------------SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEkLTDEEVDE---------MIREADIDGDGQVN 2676
Cdd:cd16179    172 nflcrpifkgagklTREDIDRVFALYDRDNNGTIENEELTGFLKDLLE-LVQEDYDEqdleefkeiILRGWDFNNDGKIS 250
EF-hand_9 pfam14658
EF-hand domain;
2555-2613 9.83e-06

EF-hand domain;


Pssm-ID: 405361  Cd Length: 66  Bit Score: 45.49  E-value: 9.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2555 FSLFDKDGDGTITTKELGTVMRSLGQN-PTEAELQDMINEVDADG-NGTIDFPEFLTMMAR 2613
Cdd:pfam14658    4 FEVCDTQKTGRVPVSRLIDYLRAVTGQdPQESRLQTLARELDPDGeDALVDLDTFLRVMRD 64
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
789-824 1.02e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.51  E-value: 1.02e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  789 CQSQHGGCHPAASCTNSPGSYKCTCPFGMNGSGFDC 824
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
2549-2658 1.18e-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 [Multi-domain]  Cd Length: 248  Bit Score: 49.49  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2549 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT----EAELQDMINEV----DADGNGTIdfpeFLTMMARKMKDTD- 2619
Cdd:cd16177     90 SEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANrpydEKKLQEYTQTIlrmfDLNGDGKL----GLSEMARLLPVQEn 165
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1514903181 2620 ----------SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE 2658
Cdd:cd16177    166 fllkfqgmklSSEEFNAIFAFYDKDGSGYIDENELDALLKDLYEKNKKE 214
EGF_CA smart00179
Calcium-binding EGF-like domain;
260-298 1.23e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 1.23e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   260 DINECE-INICSSFADCTNLPGSYRCTCPEGFVgNGLACV 298
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
175-208 1.46e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.16  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  175 DDNECARPGICHWNATCTNNPGSYVCTCNAGYKG 208
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
2530-2639 2.11e-05

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 47.25  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRNRG---LNEADQLTEeQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPE 2606
Cdd:cd16183     46 FDRDNSGtinFQEFAALWK-YITDWQNCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDD 124
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1514903181 2607 FL---TMMARkmkdtdseeeIREAFRVFDKDGNGYI 2639
Cdd:cd16183    125 FIqccVVLQT----------LTDSFRRYDTDQDGWI 150
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1074-1106 2.19e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 2.19e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1074 DVDECLNNSACSDNSICVNTEGSFLCLCDDGFS 1106
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
175-211 2.52e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 2.52e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1514903181   175 DDNECARPGICHWNATCTNNPGSYVCTCNAGYKGNGN 211
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
870-900 2.60e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 2.60e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1514903181   870 DVDECLSPSICRNNMTCQNFPGTYTCTCTVG 900
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
2600-2678 2.61e-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: 45.24  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2600 GTIDFPEFLTMMARKMKdtdSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK---LTDEEVDEMIREADIDGDGQVN 2676
Cdd:cd16253     15 DSFDHKAFFKAVGLSKK---SPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGarvLSDKETKNFLAAGDSDGDGKIG 91

                   ..
gi 1514903181 2677 YE 2678
Cdd:cd16253     92 VD 93
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
260-292 3.47e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  260 DINECE-INICSSFADCTNLPGSYRCTCPEGFVG 292
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
2530-2612 3.50e-05

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: 44.81  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRNrgLNEADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSL---GQNPTEAELQDMINEVDADGNGTIDFPE 2606
Cdd:cd16254     17 FDYKK--FFEMVGLKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFspdGRDLSDKETKALLAAGDKDGDGKIGIDE 94

                   ....*.
gi 1514903181 2607 FLTMMA 2612
Cdd:cd16254     95 FATLVA 100
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
951-990 3.64e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 3.64e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  951 DINECSQSGACPKLSTCFNTEGSYHCDCWEGYQynGIHCE 990
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
870-909 4.14e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.62  E-value: 4.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  870 DVDECLSPSICRNNMTCQNFPGTYTCTCTVGlvYDLGTCV 909
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPG--YTGRNCE 38
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
2551-2650 4.59e-05

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: 45.83  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2551 FKEAfslfDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN-GTIDFPEFLT---MMARKmkdtdseeeiRE 2626
Cdd:cd16205      6 FEEA----DKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDDNqGTLDFEEFCAfykMMSTR----------RE 71
                           90       100
                   ....*....|....*....|....*.
gi 1514903181 2627 AFRVFDK--DGNGYISAAELRHVMTN 2650
Cdd:cd16205     72 LYLLLLSysNKKDYLTLEDLARFLEV 97
EGF_CA smart00179
Calcium-binding EGF-like domain;
1158-1197 5.27e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.27e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181  1158 DIDECSGSNNesiCQPHSTCVNVPGSYKCDCNLGFLLNRT 1197
Cdd:smart00179    1 DIDECASGNP---CQNGGTCVNTVGSYRCECPPGYTDGRN 37
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
2548-2676 5.35e-05

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, 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 His-Asp-Glu-Leu (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: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 47.66  E-value: 5.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2548 IAEFKEAFSLFDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSE 2621
Cdd:cd16230    122 LARDERRFRVADQDGDSMATREELTAFL-----HPEEFPhmrdivVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEP 196
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2622 ---EEIREAFRVF-DKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVN 2676
Cdd:cd16230    197 awvQTERQQFRQFrDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLS 255
EGF_CA pfam07645
Calcium-binding EGF domain;
544-574 5.64e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.22  E-value: 5.64e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  544 DIDECEN-QKPCHQNGTCLNLAGSFSCTCKHG 574
Cdd:pfam07645    1 DVDECATgTHNCPANTVCVNTIGSFECRCPDG 32
EFh_PEF_CAPN3 cd16190
Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), ...
2546-2639 5.67e-05

Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), or calpain L3, or calpain p94, or muscle-specific calcium-activated neutral protease 3, or new calpain 1 (nCL-1), is a calpain large subunit that is mainly expressed in skeletal muscle, or lens. The skeletal muscle-specific CAPN3 are pathologically associated with limb girdle muscular dystrophy type 2A (LGMD2A). Its autolytic activity can be positively regulated by calmodulin (CaM), a known transducer of the calcium signal. CAPN3 is also involved in human melanoma tumorigenesis and progression. It impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells. Moreover, it plays an important role in sarcomere remodeling and mitochondrial protein turnover. Furthermore, the phosphorylated skeletal muscle-specific CAPN3 acts as a myofibril structural component and may participate in myofibril-based signaling pathways. In the eye, the lens-specific CAPN3, together with CAPN2, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. CAPN3 exists as a homodimer, rather than a heterodimer with the calpain small subunit. It may also form heterodimers with other calpain large subunits. CAPN3 contains a long N-terminal region, 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. Ca2+ binding at EF5 of the CAPN3 PEF domain is a distinct feature not observed in other calpain isoforms.


Pssm-ID: 320065 [Multi-domain]  Cd Length: 169  Bit Score: 46.01  E-value: 5.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2546 EQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNpTEAELQDMINEVDADGNGTIDFPEFLTMMARKmkdtdseEEIR 2625
Cdd:cd16190     70 NKIKQWQKIFKRYDTDKSGTINSYEMRNAVNDAGFR-LNNQLYDIITMRYADKHMNIDFDSFICCFVRL-------EGMF 141
                           90
                   ....*....|....
gi 1514903181 2626 EAFRVFDKDGNGYI 2639
Cdd:cd16190    142 RAFHAFDKDGDGII 155
EGF_CA smart00179
Calcium-binding EGF-like domain;
459-492 5.76e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 5.76e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   459 DVNECLvDNGGCRNRAKCVNSMGSFSCTCPSGFQ 492
Cdd:smart00179    1 DIDECA-SGNPCQNGGTCVNTVGSYRCECPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
269-297 6.39e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 42.20  E-value: 6.39e-05
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  269 CSSFADCTNLPGSYRCTCPEGFVGNGLAC 297
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
459-495 6.70e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 6.70e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1514903181  459 DVNECLvDNGGCRNRAKCVNSMGSFSCTCPSGFQLVN 495
Cdd:cd00054      1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
428-454 7.12e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.12e-05
                           10        20
                   ....*....|....*....|....*..
gi 1514903181  428 CHVNALCINVPGKFNCSCMVGYTGDGV 454
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGV 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
592-622 7.41e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.82  E-value: 7.41e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1514903181  592 GMCHLQANCYNYPGEFMCICHQGFNGDGFTC 622
Cdd:pfam12947    6 GGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1282-1321 8.44e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 8.44e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181  1282 DNNECAKNTTCHPLARCWNTVGSFTCQCRLGYAgNGTYCK 1321
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1158-1196 8.91e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.85  E-value: 8.91e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1514903181 1158 DIDECSGSNnesICQPHSTCVNVPGSYKCDCNLGFLLNR 1196
Cdd:cd00054      1 DIDECASGN---PCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EFh_PI-PLCeta2 cd16221
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ...
2552-2614 9.09e-05

EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), 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 pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 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: 320051 [Multi-domain]  Cd Length: 141  Bit Score: 44.92  E-value: 9.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN-GTIDFPEFLT---MMARK 2614
Cdd:cd16221      3 KQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNqGTLGFEEFCAfykMMSTR 69
EGF_CA smart00179
Calcium-binding EGF-like domain;
1322-1353 9.32e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 9.32e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181  1322 DIDECSTSSLrCHKSSQCINTPGSYICVCAPG 1353
Cdd:smart00179    1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPG 31
EGF_CA pfam07645
Calcium-binding EGF domain;
299-329 9.87e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.45  E-value: 9.87e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  299 DINEC-DRKNNCDPNAICTNLLGSYQCSCRSG 329
Cdd:pfam07645    1 DVDECaTGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
748-783 1.04e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 41.43  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181  748 CESGVNSCSKFAQCDNTIGSHLCFCLNGFTGDGKNC 783
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
93-133 1.35e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.46  E-value: 1.35e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181    93 DIDECTTGlHSCHGKAICSNTLGSYTCSCLNGYFgDGFQCQ 133
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
418-452 1.39e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  418 DVDECAIEKRCHVNALCINVPGKFNCSCMVGYTGD 452
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
2543-2610 1.39e-04

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 43.03  E-value: 1.39e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181  2543 LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTeaELQDMINEVDADGNGTIDFPEF-LTM 2610
Cdd:smart00027    4 ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQT--LLAKIWNLADIDNDGELDKDEFaLAM 70
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
178-211 1.41e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 41.31  E-value: 1.41e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  178 ECARPGICHWNATCTNNPGSYVCTCNAGYKGNGN 211
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDRS 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1282-1315 1.46e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181 1282 DNNECAKNTTCHPLARCWNTVGSFTCQCRLGYAG 1315
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
93-128 1.50e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.50e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1514903181   93 DIDECTTGlHSCHGKAICSNTLGSYTCSCLNGYFGD 128
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EF-hand_5 pfam13202
EF hand;
2624-2648 1.51e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 40.77  E-value: 1.51e-04
                           10        20
                   ....*....|....*....|....*
gi 1514903181 2624 IREAFRVFDKDGNGYISAAELRHVM 2648
Cdd:pfam13202    1 LKDTFRQIDLNGDGKISKEELRRLL 25
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1322-1353 1.51e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 1.51e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1322 DIDECSTSSLrCHKSSQCINTPGSYICVCAPG 1353
Cdd:cd00054      1 DIDECASGNP-CQNGGTCVNTVGSYRCSCPPG 31
EGF_CA pfam07645
Calcium-binding EGF domain;
1033-1064 1.63e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1033 DVDECATGKAQCPNASNCQNTVGWYFCECWDG 1064
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EF-hand_8 pfam13833
EF-hand domain pair;
2598-2651 1.67e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 41.53  E-value: 1.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2598 GNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL 2651
Cdd:pfam13833    1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
2624-2673 2.11e-04

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: 43.75  E-value: 2.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2624 IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDG 2673
Cdd:cd16202      2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGED 51
EGF_CA pfam07645
Calcium-binding EGF domain;
339-369 2.19e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.19e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  339 DIDECA-ASNICPSNAVCVNTAGSFFCDCGQG 369
Cdd:pfam07645    1 DVDECAtGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
1074-1104 2.23e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.23e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1074 DVDECLNNSA-CSDNSICVNTEGSFLCLCDDG 1104
Cdd:pfam07645    1 DVDECATGTHnCPANTVCVNTIGSFECRCPDG 32
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
2555-2678 2.34e-04

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, 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 is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 45.70  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2555 FSLFDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI---R 2625
Cdd:cd16228    124 FKMADKDGDLRATKEEFTAFL-----HPEEYDymkdivVLETMEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVkteR 198
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2626 EAFRVF-DKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYE 2678
Cdd:cd16228    199 EQFTEFrDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKE 252
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
2552-2607 2.40e-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: 43.47  E-value: 2.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2552 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN-GTIDFPEF 2607
Cdd:cd16220      3 KQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENqGTLTFEEF 59
EGF_CA smart00179
Calcium-binding EGF-like domain;
1033-1073 2.42e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 2.42e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1033 DVDECATGkAQCPNASNCQNTVGWYFCECWDGYTGNQTvCE 1073
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTDGRN-CE 39
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
2659-2707 2.51e-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: 40.44  E-value: 2.51e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1514903181  2659 EVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftEFVQMMTAK 2707
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFE--------------------EFKDLLKAL 29
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
547-583 2.70e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.54  E-value: 2.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1514903181  547 ECENQKPCHQNGTCLNLAGSFSCTCKHGFSGNGvTCE 583
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDR-SCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1117-1156 3.34e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.34e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1117 DIDECidEFGPLCTNG-TCINTIGSFHCVCDMGFwSNDTRC 1156
Cdd:smart00179    1 DIDEC--ASGNPCQNGgTCVNTVGSYRCECPPGY-TDGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
744-783 3.41e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   744 DVDECESGvNSCSKFAQCDNTIGSHLCFCLNGFTgDGKNC 783
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
379-416 3.51e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 3.51e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1514903181   379 DVDECAIRH-CSPYSSCENLPGSFICSCIAGFEgDGLIC 416
Cdd:smart00179    1 DIDECASGNpCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
2535-2678 3.67e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 45.12  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2535 RGLNEADQLT----EEQIAEFKEAFSLFDKDGDGTITTKELGT-VMRSLGQNPTEaELQDMINEVDADGNGTIDFPEF-L 2608
Cdd:cd16224     18 GGEEDADEFAklspEEQQKRLKSIIKKIDTDSDGFLTEEELSSwIQQSFRHYALE-DAKQQFPEYDKDGDGAVTWDEYnM 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2609 TMMARKM---KDT---DSEEE---------------------------------------------IREAFRVFDKDGNG 2637
Cdd:cd16224     97 QMYDRVIdydEDTvldDEEEEsfrqlhlkdkkrfdkantdggpglnltefiafehpeevdymtefvIQEALEEHDKDGDG 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1514903181 2638 YISAAELrhvmtnLGEKLTD-----------EEVDEMIREADIDGDGQVNYE 2678
Cdd:cd16224    177 FISLEEF------LGDYRKDptanedpewiiVEKDRFVNDYDKDNDGKLDPQ 222
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
2529-2639 4.07e-04

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


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 43.37  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2529 CFDHRNRG---LNEADQLTEEqIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQnPTEAELQDMINEVDADGNGTIDFP 2605
Cdd:cd16182     50 LMDTNGSGrldLEEFKTLWSD-LKKWQAIFKKFDTDRSGTLSSYELRKALESAGF-HLSNKVLQALVLRYADSTGRITFE 127
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1514903181 2606 EFLTMMARkmkdtdseeeIREAFRVF---DKDGNGYI 2639
Cdd:cd16182    128 DFVSCLVR----------LKTAFETFsalDKKNEGVI 154
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
2551-2607 4.27e-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: 40.67  E-value: 4.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTeaELQDMINEVDADGNGTIDFPEF 2607
Cdd:cd00052      1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRS--VLAQIWDLADTDKDGKLDKEEF 55
EGF_CA smart00179
Calcium-binding EGF-like domain;
826-869 4.58e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.92  E-value: 4.58e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1514903181   826 DVDECNEnstlPHNCSLLAMCNNTEGSYICKCMEGYLgDGFTCE 869
Cdd:smart00179    1 DIDECAS----GNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
991-1019 4.85e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.85e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  991 DINECSVGNFICPDNSTCYNKEGGYNCPC 1019
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA pfam07645
Calcium-binding EGF domain;
2369-2397 4.94e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 4.94e-04
                           10        20
                   ....*....|....*....|....*....
gi 1514903181 2369 DLDECKTNEAPCSKTAQCVNTYGGYRCVC 2397
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA pfam07645
Calcium-binding EGF domain;
826-860 5.56e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 5.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  826 DVDECNensTLPHNCSLLAMCNNTEGSYICKCMEG 860
Cdd:pfam07645    1 DVDECA---TGTHNCPANTVCVNTIGSFECRCPDG 32
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
2559-2613 5.57e-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: 40.94  E-value: 5.57e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2559 DKDGD-GTIT--------TKELGTVMRSLGQNPTeaeLQDMINEVDADGNGTIDFPEFLTMMAR 2613
Cdd:cd00213     19 GKEGDkDTLSkkelkellETELPNFLKNQKDPEA---VDKIMKDLDVNKDGKVDFQEFLVLIGK 79
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
2205-2234 5.61e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 39.50  E-value: 5.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181 2205 PCHEMADCTSTGYNYTCKCKRGYAGNGKEC 2234
Cdd:pfam12947    7 GCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
2626-2676 5.68e-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: 40.28  E-value: 5.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1514903181 2626 EAFRVFDKDGNGYISAAELRHVMTNLGekLTDEEVDEMIREADIDGDGQVN 2676
Cdd:cd00052      3 QIFRSLDPDGDGLISGDEARPFLGKSG--LPRSVLAQIWDLADTDKDGKLD 51
EGF_CA smart00179
Calcium-binding EGF-like domain;
785-816 5.74e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.54  E-value: 5.74e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1514903181   785 DINECQSQHGgCHPAASCTNSPGSYKCTCPFG 816
Cdd:smart00179    1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPG 31
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
2544-2673 5.77e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 44.60  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2544 TEEQIAEFKEAFSLFDKDGDGTITTKELGTvMRSLGQNPT--EAELQDMINEVDADGNGTIDFPEFLTMMAR------KM 2615
Cdd:cd16225    126 DKEVLDRYKDRWSQADEPEDGLLDVEEFLS-FRHPEHSRGmlKNMVKEILHDLDQDGDEKLTLDEFVSLPPGtveeqqAE 204
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1514903181 2616 KDTDSEEEIREAFR-VFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDG 2673
Cdd:cd16225    205 DDDEWKKERKKEFEeVIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDG 263
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
2548-2639 6.32e-04

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


Pssm-ID: 320063 [Multi-domain]  Cd Length: 169  Bit Score: 42.81  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2548 IAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEaELQDMINEVDADGNGTIDFPEFLTMMARKmkdtdseEEIREA 2627
Cdd:cd16188     72 IKKWQGIYKQFDTDRSGTIGSQELPGAFEAAGFHLNE-QLYQMIIRRYSDEDGNMDFDNFISCLVRL-------DAMFRA 143
                           90
                   ....*....|..
gi 1514903181 2628 FRVFDKDGNGYI 2639
Cdd:cd16188    144 FKSLDKDGTGQI 155
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
2539-2676 6.60e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 44.21  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2539 EADQLTEE-QIAEFKEAFSLFDKDGDGTITTKELGTVMRslgqNPTEAELQDMINE-------VDADGNGTIDF----PE 2606
Cdd:cd16225     23 EFEEDSEPkKRKKLKEIFKKVDVNTDGFLSAEELEDWIM----EKTQEHFQEAVEEneqifkaVDTDKDGNVSWeeyrVH 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2607 FLTMM---------------ARKMKDTDSEEEIREAFRVF--DKDGNGYISAAEL---RHVMTNLG--EKLtdeeVDEMI 2664
Cdd:cd16225     99 FLLSKgyseeeaeekiknneELKLDEDDKEVLDRYKDRWSqaDEPEDGLLDVEEFlsfRHPEHSRGmlKNM----VKEIL 174
                          170
                   ....*....|..
gi 1514903181 2665 READIDGDGQVN 2676
Cdd:cd16225    175 HDLDQDGDEKLT 186
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
2590-2677 6.74e-04

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


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 42.96  E-value: 6.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2590 MINEVDADGNGTIDFPEF--LTMMARKMKDtdseeeireAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMI-RE 2666
Cdd:cd16196     46 MVAMMDVDRSGKLGFEEFkkLWEDLRSWKR---------VFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVlRY 116
                           90
                   ....*....|.
gi 1514903181 2667 AdiDGDGQVNY 2677
Cdd:cd16196    117 S--NKDGRISF 125
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
785-816 6.81e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 6.81e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  785 DINECQSQHGgCHPAASCTNSPGSYKCTCPFG 816
Cdd:cd00054      1 DIDECASGNP-CQNGGTCVNTVGSYRCSCPPG 31
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
2556-2678 7.21e-04

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 43.97  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2556 SLFDKDgdgTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEF--LTMMARKMKdtdSEEEIREAFRVFDK 2633
Cdd:cd15899      9 SDYDHE---AFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELhsWILESFKRH---AMEESKEQFRAVDP 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514903181 2634 DGNGYISAAELRHVMtnLGEKLTDEE-------VDE-----------MIREADIDGDGQVNYE 2678
Cdd:cd15899     83 DEDGHVSWDEYKNDT--YGSVGDDEEnvadnikEDEeykklllkdkkRFEAADQDGDLILTLE 143
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
2590-2681 7.23e-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: 42.58  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2590 MINEVDADGNGTIDFPEFLTM--MARKMKDTdseeeireaFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM-IRE 2666
Cdd:cd16195     48 MVALMDLSVNGRLSLEEFSRLwkKLRKYKDI---------FQKADVSKSGFLSLSELRNAIQAAGIRVSDDLLNLMaLRY 118
                           90
                   ....*....|....*
gi 1514903181 2667 AdiDGDGQVNYEGHV 2681
Cdd:cd16195    119 G--DSSGRISFESFI 131
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
379-412 7.97e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 7.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  379 DVDECAIRH-CSPYSSCENLPGSFICSCIAGFEGD 412
Cdd:cd00054      1 DIDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
418-450 8.51e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 8.51e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1514903181   418 DVDECAIEKRCHVNALCINVPGKFNCSCMVGYT 450
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT 33
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
2530-2644 9.53e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 43.58  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRNR----GLN-----------EADQLTEEQIaefKEAFSLFDKDGDGTITTKE-LGTVMRSLGQNPTE----AELQD 2589
Cdd:cd16224    130 FDKANTdggpGLNltefiafehpeEVDYMTEFVI---QEALEEHDKDGDGFISLEEfLGDYRKDPTANEDPewiiVEKDR 206
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1514903181 2590 MINEVDADGNGTIDFPEFLTMMARKMKDTDSEEE---IREafrvFDKDGNGYISAAEL 2644
Cdd:cd16224    207 FVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEAlhlIDE----MDLNGDGRLSEEEI 260
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1117-1149 9.71e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 9.71e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181 1117 DIDECiDEFGPLCTNGTCINTIGSFHCVCDMGF 1149
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGY 32
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
2536-2638 1.00e-03

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 42.36  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2536 GLNEADQLTEeQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgNGTIDFPEFLTMMARKM 2615
Cdd:cd16181     58 GFNEFKELWA-ALNQWKTTFMQYDRDRSGTVEPQELQQAIRSFGYNLSPQALNVIVKRYSK--NGRITFDDFVACAVRLR 134
                           90       100
                   ....*....|....*....|...
gi 1514903181 2616 KDTDseeeireAFRVFDKDGNGY 2638
Cdd:cd16181    135 ALTD-------RFRRRDTQQNGT 150
EF-hand_5 pfam13202
EF hand;
2551-2575 1.10e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 38.45  E-value: 1.10e-03
                           10        20
                   ....*....|....*....|....*
gi 1514903181 2551 FKEAFSLFDKDGDGTITTKELGTVM 2575
Cdd:pfam13202    1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
2546-2637 1.30e-03

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: 41.80  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2546 EQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVdADGNGTIDFPEFLTMMAR--KMKDTdseee 2623
Cdd:cd16196     68 EDLRSWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVLRY-SNKDGRISFDDFIMCAVKlkTMFEI----- 141
                           90
                   ....*....|....
gi 1514903181 2624 ireaFRVFDKDGNG 2637
Cdd:cd16196    142 ----FKEKDPRGGG 151
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
2530-2639 1.49e-03

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


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 41.87  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRNRG---LNEADQLTEeQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPE 2606
Cdd:cd16184     46 FDKDKSGtidIYEFQALWN-YIQQWKQVFQQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRARRSLTLDQ 124
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1514903181 2607 F--LTMMARKMKDtdseeeireAFRVFDKDGNGYI 2639
Cdd:cd16184    125 FiqVCVQLQSLTD---------AFRQRDTQMTGTI 150
EGF_CA smart00179
Calcium-binding EGF-like domain;
584-623 1.54e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 1.54e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   584 DINECAIEGMCHLQANCYNYPGEFMCICHQGFNgDGFTCT 623
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
302-335 1.55e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 38.23  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  302 ECDRKNNCDPNAICTNLLGSYQCSCRSGFLGTGT 335
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDRS 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
584-618 1.84e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 1.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181  584 DINECAIEGMCHLQANCYNYPGEFMCICHQGFNGD 618
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGR 35
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
2547-2643 1.92e-03

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: 41.42  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2547 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGqNPTEAELQDMINEVDADGNGTIDFPEFLTMMAR--KMKDtdseeei 2624
Cdd:cd16195     71 KLRKYKDIFQKADVSKSGFLSLSELRNAIQAAG-IRVSDDLLNLMALRYGDSSGRISFESFICLMLRleCMAK------- 142
                           90       100
                   ....*....|....*....|
gi 1514903181 2625 reAFRVFDKDGNG-YISAAE 2643
Cdd:cd16195    143 --IFRNLSKDGGGiYLTESE 160
EGF_CA pfam07645
Calcium-binding EGF domain;
1322-1353 2.00e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.99  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1322 DIDECSTSSLRCHKSSQCINTPGSYICVCAPG 1353
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EFh_PEF_CAPN1_like cd16189
Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1), m-type calpain (CAPN2) ...
2547-2639 2.23e-03

Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1), m-type calpain (CAPN2), and similar proteins; The family includes mu-type calpain (CAPN1) and m-type calpain (CAPN2), both of which are ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine proteases that 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 catalytic subunit CAPN1 or CAPN2 in complex with a regulatory subunit encoded by CAPNS1 forms a mu- or m-calpain heterodimer, respectively.


Pssm-ID: 320064 [Multi-domain]  Cd Length: 168  Bit Score: 41.19  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2547 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAeLQDMINEVDADGNGTIDFPEFLTMMARKmkdtdseEEIRE 2626
Cdd:cd16189     71 KIQKYLKIYKKFDTDGSGTMSSYEMRLALEEAGFKLNNQ-LHQVLVARYADQELTIDFDNFVRCLVRL-------ELLFK 142
                           90
                   ....*....|...
gi 1514903181 2627 AFRVFDKDGNGYI 2639
Cdd:cd16189    143 IFKQLDKDNTGTI 155
EGF_CA pfam07645
Calcium-binding EGF domain;
418-448 2.27e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.60  E-value: 2.27e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  418 DVDECAIEKR-CHVNALCINVPGKFNCSCMVG 448
Cdd:pfam07645    1 DVDECATGTHnCPANTVCVNTIGSFECRCPDG 32
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
2659-2706 2.36e-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: 37.38  E-value: 2.36e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1514903181 2659 EVDEMIREADIDGDGQVNYEghvrnlviiqkrtnpfsvftEFVQMMTA 2706
Cdd:pfam00036    1 ELKEIFRLFDKDGDGKIDFE--------------------EFKELLKK 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
744-783 2.52e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 2.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1514903181  744 DVDECESGvNSCSKFAQCDNTIGSHLCFCLNGFTgdGKNC 783
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNC 37
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1285-1318 2.64e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.46  E-value: 2.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181 1285 ECAKNTTCHPLARCWNTVGSFTCQCRLGYAGNGT 1318
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDRS 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
463-492 2.65e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 37.58  E-value: 2.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1514903181  463 CLVDNGGCRNRAKCVNSMGSFSCTCPSGFQ 492
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYT 30
EGF_CA pfam07645
Calcium-binding EGF domain;
870-900 2.87e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.22  E-value: 2.87e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  870 DVDECLSPS-ICRNNMTCQNFPGTYTCTCTVG 900
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
2530-2612 2.88e-03

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: 39.47  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2530 FDHRnrGLNEADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNP---TEAELQDMINEVDADGNGTIDFPE 2606
Cdd:cd16253     17 FDHK--AFFKAVGLSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGArvlSDKETKNFLAAGDSDGDGKIGVDE 94

                   ....*.
gi 1514903181 2607 FLTMMA 2612
Cdd:cd16253     95 FKSMVK 100
EGF_CA pfam07645
Calcium-binding EGF domain;
1117-1148 2.96e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.22  E-value: 2.96e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181 1117 DIDECIDEFGPLCTNGTCINTIGSFHCVCDMG 1148
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
2576-2679 3.01e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes 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 then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 40.31  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2576 RSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARkMKDtdsEEEIREAFRVFDKDGNGYISAAELRHVMTNL-GEK 2654
Cdd:cd16207     29 RRLHINCSESYLRELFDKADTDKKGYLNFEEFQEFVKL-LKR---RKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVqKED 104
                           90       100
                   ....*....|....*....|....*....
gi 1514903181 2655 LTDEEVDEM----IREADIDGDGQVNYEG 2679
Cdd:cd16207    105 VDRETWEKIfekfARRIDDSDSLTMTLEG 133
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1201-1241 3.16e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1514903181 1201 DIDEClADESPCTANAGCVNSAGSFQCPCASGFEaqGPKCI 1241
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
216-259 3.62e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.23  E-value: 3.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1514903181   216 DIDECsETPGVCSaffGYKGCKNLPGSYTCLCNSGYQsNGQTCE 259
Cdd:smart00179    1 DIDEC-ASGNPCQ---NGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1033-1067 3.74e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1514903181 1033 DVDECATGkAQCPNASNCQNTVGWYFCECWDGYTG 1067
Cdd:cd00054      1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
826-869 3.93e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 3.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1514903181  826 DVDECnensTLPHNCSLLAMCNNTEGSYICKCMEGYLGDgfTCE 869
Cdd:cd00054      1 DIDEC----ASGNPCQNGGTCVNTVGSYRCSCPPGYTGR--NCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1201-1241 4.58e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.58e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1514903181  1201 DIDEClADESPCTANAGCVNSAGSFQCPCASGFEaQGPKCI 1241
Cdd:smart00179    1 DIDEC-ASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
704-743 4.86e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 4.86e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1514903181   704 DIDECEENVCPKKETQCVNNPGSFDCICKVGYTlNGTECI 743
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EF-hand_5 pfam13202
EF hand;
2587-2611 5.27e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 5.27e-03
                           10        20
                   ....*....|....*....|....*
gi 1514903181 2587 LQDMINEVDADGNGTIDFPEFLTMM 2611
Cdd:pfam13202    1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
2587-2672 5.28e-03

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


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 39.52  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2587 LQDMINEVDADGNGTIDFPE---FLTMMARKMkdtdSEEEIREAFRVFDKDGNGYISAAELrhvmTNLGEKLTD-EEVDE 2662
Cdd:cd16202      2 LKDQFRKADKNGDGKLSFKEckkLLKKLNVKV----DKDYAKKLFQEADTSGEDVLDEEEF----VQFYNRLTKrPEIEE 73
                           90
                   ....*....|
gi 1514903181 2663 MIREADIDGD 2672
Cdd:cd16202     74 LFKKYSGDDE 83
PLN02964 PLN02964
phosphatidylserine decarboxylase
2621-2691 5.37e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 5.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1514903181 2621 EEEIREAFRVF---DKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKRT 2691
Cdd:PLN02964   175 ETERSFARRILaivDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQE 248
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
342-375 5.98e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.69  E-value: 5.98e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1514903181  342 ECAASNICPSNAVCVNTAGSFFCDCGQGYNFSRN 375
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDRS 34
EGF_CA pfam07645
Calcium-binding EGF domain;
459-490 6.00e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.45  E-value: 6.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  459 DVNECLVDNGGCRNRAKCVNSMGSFSCTCPSG 490
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
260-289 6.00e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.45  E-value: 6.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1514903181  260 DINECEI--NICSSFADCTNLPGSYRCTCPEG 289
Cdd:pfam07645    1 DVDECATgtHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
501-534 6.03e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 6.03e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1514903181   501 DIDECQLPEkACGTNEQCSNMEGSYACHCKEGFT 534
Cdd:smart00179    1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
2515-2676 6.30e-03

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


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 41.01  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2515 NFPQELGTLgwysvcfdHRNRGLNEADQLTEEQIAEFKEAFslfDKDGDGTITTKELGTVMrslgqnPTE---------- 2584
Cdd:cd16177     23 NFFRELERA--------RRGAGVDSKSANFGEKMKEFMQKY---DKNADGRIEMAELAQIL------PTEenfllcfrqh 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514903181 2585 ----AELQDMINEVDADGNGTIDFPE---FLTMMARKMKDTDSEEEIRE----AFRVFDKDGNGYISAAE---LRHVMTN 2650
Cdd:cd16177     86 vgssSEFMEAWRKYDTDRSGYIEANElkgFLSDLLKKANRPYDEKKLQEytqtILRMFDLNGDGKLGLSEmarLLPVQEN 165
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1514903181 2651 L-----GEKLTDEEVDEMIREADIDGDGQVN 2676
Cdd:cd16177    166 FllkfqGMKLSSEEFNAIFAFYDKDGSGYID 196
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
2624-2690 6.35e-03

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: 39.19  E-value: 6.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1514903181 2624 IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEGHVRNLVIIQKR 2690
Cdd:cd15898      2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTER 68
EGF_CA pfam07645
Calcium-binding EGF domain;
704-734 6.76e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.45  E-value: 6.76e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1514903181  704 DIDECEE--NVCPKKETqCVNNPGSFDCICKVG 734
Cdd:pfam07645    1 DVDECATgtHNCPANTV-CVNTIGSFECRCPDG 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
388-416 8.48e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 36.04  E-value: 8.48e-03
                           10        20
                   ....*....|....*....|....*....
gi 1514903181  388 CSPYSSCENLPGSFICSCIAGFEGDGLIC 416
Cdd:pfam12947    8 CHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
 
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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