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Conserved domains on  [gi|2493458|sp|Q26678|]
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RecName: Full=Flagellar calcium-binding protein TB-44A; AltName: Full=44 kDa calcimedin; AltName: Full=44 kDa calflagin

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein similar to Homo sapiens guanylyl cyclase-activating proteins (GCAP1 and GCAP2), myosin regulatory light chain proteins, (MYL2, MYL5, MYL9, MYL10, and MYL12), and Kv channel-interacting proteins (KChIP1, KChIP2 and KChIP4)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
47-192 1.97e-13

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 1.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   47 AESKSRRIELFKRFDTNGTGKLSfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 126
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  127 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALpkwKEWGVDITDATTVFNEIDTNGSGVVTFDEF 192
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLL---TALGVSEEEADELFARLDTDGDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
236-381 1.00e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 64.81  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  236 AESKSRRIELFKQFDTNGTGKLGfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 315
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  316 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALKkwkEWGVDITDATTVFNEIDTNGSGVVTFDEF 381
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLT---ALGVSEEEADELFARLDTDGDGKISFEEF 125
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
47-192 1.97e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 1.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   47 AESKSRRIELFKRFDTNGTGKLSfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 126
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  127 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALpkwKEWGVDITDATTVFNEIDTNGSGVVTFDEF 192
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLL---TALGVSEEEADELFARLDTDGDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
236-381 1.00e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 64.81  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  236 AESKSRRIELFKQFDTNGTGKLGfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 315
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  316 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALKkwkEWGVDITDATTVFNEIDTNGSGVVTFDEF 381
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLT---ALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 323-384 3.68e-10

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: 55.25  E-value: 3.68e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493458  323 ELTVMFDTMDKDGSLLLELQEFKEALKKwKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCW 384
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 134-195 9.32e-10

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: 54.09  E-value: 9.32e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493458  134 ELTVMFDTMDKDGSLLLELQEFKEALPKwKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCW 195
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
327-381 4.40e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458    327 MFDTMDKDGSLLLELQEFKEALKKWKEwGVDITDA--TTVFNEIDTNGSGVVTFDEF 381
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEE-GEPLSDEevEELFKEFDLDKDGRISFEEF 62
EF-hand_7 pfam13499
EF-hand domain pair;
138-192 4.67e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 4.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458    138 MFDTMDKDGSLLLELQEFKEALPKWKEwGVDITDA--TTVFNEIDTNGSGVVTFDEF 192
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEE-GEPLSDEevEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
47-192 1.97e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 1.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   47 AESKSRRIELFKRFDTNGTGKLSfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 126
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  127 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALpkwKEWGVDITDATTVFNEIDTNGSGVVTFDEF 192
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLL---TALGVSEEEADELFARLDTDGDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
236-381 1.00e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 64.81  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  236 AESKSRRIELFKQFDTNGTGKLGfrevldgcysilkLDEFTTHLPDIVQRAFDKAKDLGNkvkgvGEEDLVEFLEFRLML 315
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLE-------------RDDFEALFRRLWATLFSEADTDGD-----GRISREEFVAGMESL 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2493458  316 CYIYDIFELTVMFDTMDKDGSLLLELQEFKEALKkwkEWGVDITDATTVFNEIDTNGSGVVTFDEF 381
Cdd:COG5126  63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLT---ALGVSEEEADELFARLDTDGDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 323-384 3.68e-10

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: 55.25  E-value: 3.68e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493458  323 ELTVMFDTMDKDGSLLLELQEFKEALKKwKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCW 384
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 134-195 9.32e-10

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: 54.09  E-value: 9.32e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493458  134 ELTVMFDTMDKDGSLLLELQEFKEALPKwKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCW 195
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
327-381 4.40e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458    327 MFDTMDKDGSLLLELQEFKEALKKWKEwGVDITDA--TTVFNEIDTNGSGVVTFDEF 381
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEE-GEPLSDEevEELFKEFDLDKDGRISFEEF 62
EF-hand_7 pfam13499
EF-hand domain pair;
138-192 4.67e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 4.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458    138 MFDTMDKDGSLLLELQEFKEALPKWKEwGVDITDA--TTVFNEIDTNGSGVVTFDEF 192
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEE-GEPLSDEevEELFKEFDLDKDGRISFEEF 62
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 54-192 5.11e-05

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 43.29  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   54 IELFKRFDTNGTGKLSFRE----VLDGCYSILKLDefTTHLpdiVQRAFDKAKDLGnkvkgvgeedlVEFLEFRLMLCYI 129
Cdd:cd16180   3 RRIFQAVDRDRSGRISAKElqraLSNGDWTPFSIE--TVRL---MINMFDRDRSGT-----------INFDEFVGLWKYI 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2493458  130 YDIFELtvmFDTMDKDGSLLLELQEFKEALpkwKEWGVDITDATT--VFNEIDTNGSGVVTFDEF 192
Cdd:cd16180  67 QDWRRL---FRRFDRDRSGSIDFNELQNAL---SSFGYRLSPQFVqlLVRKFDRRRRGSISFDDF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
135-351 9.78e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 9.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  135 LTVMFDTMDKDGSLLLELQEFKEALPKWKEwgvditdatTVFNEIDTNGSGVVTFDEFscwavtkklqvcgdpdgegaak 214
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWA---------TLFSEADTDGDGRISREEF---------------------- 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  215 ttadrkVAWERIRCAIPRDKDAEsksrriELFKQFDTNGTGKLGfrevldgcysilkLDEFTTHLPDIvqrafdkakdlg 294
Cdd:COG5126  56 ------VAGMESLFEATVEPFAR------AAFDLLDTDGDGKIS-------------ADEFRRLLTAL------------ 98

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458  295 nkvkGVGEEDLVEflefrlmlcyiydifeltvMFDTMDKDGSLLLELQEFKEALKKW 351
Cdd:COG5126  99 ----GVSEEEADE-------------------LFARLDTDGDGKISFEEFVAAVRDY 132
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 48-264 1.43e-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: 43.20  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   48 ESKSRRIELFKRFDTNGTGKLSFREVLDGcysILKldEFTTHLPDIVQRAFD---------------KAKDLGNKVKGVG 112
Cdd:cd15899  32 ESKRRLGVIVSKMDVDKDGFISAKELHSW---ILE--SFKRHAMEESKEQFRavdpdedghvswdeyKNDTYGSVGDDEE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  113 EEDL--VEFLEFRLMLcyiydiFELTVMFDTMDKDGSLLLELQEFKEAL-PKWKEWGVDITDATTVfNEIDTNGSGVVTF 189
Cdd:cd15899 107 NVADniKEDEEYKKLL------LKDKKRFEAADQDGDLILTLEEFLAFLhPEESPYMLDFVIKETL-EDLDKNGDGFISL 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  190 DEF-------------SCWAVTKKLQVCGDPDGEGAAKTTADRKVAWerircAIPRDKD-AESKSRriELFKQFDTNGTG 255
Cdd:cd15899 180 EEFisdpysadeneeePEWVKVEKERFVELRDKDKDGKLDGEELLSW-----VDPSNQEiALEEAK--HLIAESDENKDG 252


                ....*....
gi 2493458  256 KLGFREVLD 264
Cdd:cd15899 253 KLSPEEILD 261
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 290-382 4.38e-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: 40.67  E-value: 4.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  290 AKDLGNKVKGVGEEDLVEFLEFRLMLCYIydifeltvMFDTMDKDGSLLLELQEFKEALKKWKEWgvditdaTTVFNEID 369
Cdd:cd16182  18 AVELQKLLNASLLKDMPKFDGFSLETCRS--------LIALMDTNGSGRLDLEEFKTLWSDLKKW-------QAIFKKFD 82

                        90
                ....*....|...
gi 2493458  370 TNGSGVVTFDEFS 382
Cdd:cd16182  83 TDRSGTLSSYELR 95
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 243-381 8.95e-04

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: 39.82  E-value: 8.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  243 IELFKQFDTNGTGKLGFRE----VLDGCYSILKLDefTTHLpdiVQRAFDKAKDLGnkvkgvgeedlVEFLEFRLMLCYI 318
Cdd:cd16180   3 RRIFQAVDRDRSGRISAKElqraLSNGDWTPFSIE--TVRL---MINMFDRDRSGT-----------INFDEFVGLWKYI 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2493458  319 YDIFELtvmFDTMDKDGSLLLELQEFKEALkkwKEWGVDITDATT--VFNEIDTNGSGVVTFDEF 381
Cdd:cd16180  67 QDWRRL---FRRFDRDRSGSIDFNELQNAL---SSFGYRLSPQFVqlLVRKFDRRRRGSISFDDF 125
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 327-382 3.06e-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: 37.65  E-value: 3.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2493458  327 MFDTMDKDGSLLLELQEFKEALKKWKewgVDITDATT--VFNEIDTNGSGVVTFDEFS 382
Cdd:cd15898   5 QWIKADKDGDGKLSLKEIKKLLKRLN---IRVSEKELkkLFKEVDTNGDGTLTFDEFE 59
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 101-193 3.15e-03

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


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 37.97  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  101 AKDLGNKVKGVGEEDLVEFLEFRLMLCYIydifeltvMFDTMDKDGSLLLELQEFKEALPKWKEWgvditdaTTVFNEID 180
Cdd:cd16182  18 AVELQKLLNASLLKDMPKFDGFSLETCRS--------LIALMDTNGSGRLDLEEFKTLWSDLKKW-------QAIFKKFD 82

                        90
                ....*....|...
gi 2493458  181 TNGSGVVTFDEFS 193
Cdd:cd16182  83 TDRSGTLSSYELR 95
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 327-391 3.19e-03

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: 36.04  E-value: 3.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458  327 MFDTMDKDGSLLLELQEFKEALKKWkewGVDITDATTVFNEIDTNGSGVVTFDEFS--CWAVTKKLQ 391
Cdd:cd00052   4 IFRSLDPDGDGLISGDEARPFLGKS---GLPRSVLAQIWDLADTDKDGKLDKEEFAiaMHLIALALN 67
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 237-405 4.12e-03

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: 38.82  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  237 ESKSRRIELFKQFDTNGTGKL-------------GFREV----LDGCYSILKLDEFTTHLPDIVQRAFDKAKDLGNkvkg 299
Cdd:cd16225  70 EAVEENEQIFKAVDTDKDGNVsweeyrvhfllskGYSEEeaeeKIKNNEELKLDEDDKEVLDRYKDRWSQADEPED---- 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458  300 vGEEDLVEFLEFR------LMLCYIydIFEltvMFDTMDKDGSLLLELQEF------------KEALKKWKEwgvditDA 361
Cdd:cd16225 146 -GLLDVEEFLSFRhpehsrGMLKNM--VKE---ILHDLDQDGDEKLTLDEFvslppgtveeqqAEDDDEWKK------ER 213

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 2493458  362 TTVFNE-IDTNGSGVVTFDEfscwavtkkLQVCGDPDGEENGANE 405
Cdd:cd16225 214 KKEFEEvIDLNHDGKVTKEE---------LEEYMDPRNERHALNE 249
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 55-155 4.69e-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: 37.21  E-value: 4.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493458   55 ELFKRFDTNGTGKLSFREvldgCYSILK-----LDEFTTHlpDIVQRAfdkakdlgnKVKGVGEEDLVEFLEFRLMLCYI 129
Cdd:cd16202   4 DQFRKADKNGDGKLSFKE----CKKLLKklnvkVDKDYAK--KLFQEA---------DTSGEDVLDEEEFVQFYNRLTKR 68

                        90       100
                ....*....|....*....|....*...
gi 2493458  130 YDIFELtvmFDTMDKDGSLL--LELQEF 155
Cdd:cd16202  69 PEIEEL---FKKYSGDDEALtvEELRRF 93
EF-hand_8 pfam13833
EF-hand domain pair;
342-381 5.06e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.98  E-value: 5.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2493458    342 QEFKEALKKWKEWGVDITDATTVFNEIDTNGSGVVTFDEF 381
Cdd:pfam13833   8 EELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 138-202 7.02e-03

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: 34.89  E-value: 7.02e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2493458  138 MFDTMDKDGSLLLELQEfkeALPKWKEWGVDITDATTVFNEIDTNGSGVVTFDEFS--CWAVTKKLQ 202
Cdd:cd00052   4 IFRSLDPDGDGLISGDE---ARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAiaMHLIALALN 67
EFh_PEF_CAPN11 cd16193
Penta-EF hand, calcium binding motifs, found in calpain-11 (CAPN11); CAPN11, also termed ...
 327-374 7.43e-03

Penta-EF hand, calcium binding motifs, found in calpain-11 (CAPN11); CAPN11, also termed calcium-activated neutral proteinase 11 (CANP 11), is a mammalian orthologue of micro/m calpain. It is one of the calpain large subunits that appears to be exclusively expressed in certain cells of the testis. It may be involved in regulating calcium-dependent signal transduction events during meiosis and sperm functional processes. CAPN11 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320068 [Multi-domain]  Cd Length: 169  Bit Score: 37.21  E-value: 7.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 2493458  327 MFDTMDKDGSLLLELQEFKEALKKWKEWgvditdaTTVFNEIDTNGSG 374
Cdd:cd16193  48 MINLMDKDGSGKLGLHEFKILWKKIKKW-------MEIFKECDQDRSG 88
 
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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