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Conserved domains on  [gi|2462496216|ref|XP_054188780|]
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spermatogenesis-associated protein 21 isoform X2 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040236)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 452-511 3.98e-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: 56.02  E-value: 3.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462496216 452 FRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:cd00051     2 LREAFRLFdkDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 159-384 6.22e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 6.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  159 PESCQGSGYQSTPSHQADMVQPAEPCCRLASHGQPLGgkHPKEAGVPHIRPQEaPPEPSPGGHGDSSQEAMPPMSVVAPE 238
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRR-RAARPTVGSLTSLADPPPPPPTPEPA 2711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  239 EKTVNPFLPSTPGPKKAKGGGEAVETHPAPGPLPPPEVRDIGERREPDRAQQQ-PQKPAVAAGTQSlGNFRQGFMKCLLE 317
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAA-GPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496216  318 VEKMEASHRRASKARSQTAQKSPRTLTPVPTSAPS--LPQTPASVPASGPSwarLPAPGPEPAPMGAPV 384
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgpLPPPTSAQPTAPPP---PPGPPPPSLPLGGSV 2856
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 452-511 3.98e-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: 56.02  E-value: 3.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462496216 452 FRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:cd00051     2 LREAFRLFdkDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 449-511 4.06e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 52.84  E-value: 4.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462496216 449 EEAFRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:PTZ00184   83 EEEIKEAFKVFdrDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 460-510 4.38e-05

Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.


Pssm-ID: 459805 [Multi-domain]  Cd Length: 56  Bit Score: 41.40  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462496216 460 NGPGEV---DAQSLKNILLLMGFSVTlaqveDALMSADVNGDGRVDFKDFLAVM 510
Cdd:pfam00404   4 NGDGKVnalDALLLKNYLLGSGTGSS-----INKKAADVNGDGKVNALDALLLK 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 159-384 6.22e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 6.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  159 PESCQGSGYQSTPSHQADMVQPAEPCCRLASHGQPLGgkHPKEAGVPHIRPQEaPPEPSPGGHGDSSQEAMPPMSVVAPE 238
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRR-RAARPTVGSLTSLADPPPPPPTPEPA 2711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  239 EKTVNPFLPSTPGPKKAKGGGEAVETHPAPGPLPPPEVRDIGERREPDRAQQQ-PQKPAVAAGTQSlGNFRQGFMKCLLE 317
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAA-GPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496216  318 VEKMEASHRRASKARSQTAQKSPRTLTPVPTSAPS--LPQTPASVPASGPSwarLPAPGPEPAPMGAPV 384
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgpLPPPTSAQPTAPPP---PPGPPPPSLPLGGSV 2856
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
448-512 6.62e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 6.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496216 448 QEEAFRSYFEIF--NGPGEVDAQSLKniLLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMTD 512
Cdd:COG5126    67 VEPFARAAFDLLdtDGDGKISADEFR--RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 485-511 2.36e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 2.36e-03
                           10        20
                   ....*....|....*....|....*..
gi 2462496216  485 QVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 452-511 3.98e-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: 56.02  E-value: 3.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462496216 452 FRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:cd00051     2 LREAFRLFdkDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 449-511 4.06e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 52.84  E-value: 4.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462496216 449 EEAFRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:PTZ00184   83 EEEIKEAFKVFdrDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00183 PTZ00183
centrin; Provisional
 434-511 6.53e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 49.30  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216 434 YQNREKSEEQLTLKQEEAFRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:PTZ00183    1 MRKRRSERPGLTEDQKKEIREAFDLFdtDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMT 80
PTZ00184 PTZ00184
calmodulin; Provisional
 442-510 4.24e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.06  E-value: 4.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462496216 442 EQLTLKQEEAFRSYFEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVM 510
Cdd:PTZ00184    3 DQLTEEQIAEFKEAFSLFdkDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLM 73
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 460-510 4.38e-05

Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.


Pssm-ID: 459805 [Multi-domain]  Cd Length: 56  Bit Score: 41.40  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462496216 460 NGPGEV---DAQSLKNILLLMGFSVTlaqveDALMSADVNGDGRVDFKDFLAVM 510
Cdd:pfam00404   4 NGDGKVnalDALLLKNYLLGSGTGSS-----INKKAADVNGDGKVNALDALLLK 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 159-384 6.22e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 6.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  159 PESCQGSGYQSTPSHQADMVQPAEPCCRLASHGQPLGgkHPKEAGVPHIRPQEaPPEPSPGGHGDSSQEAMPPMSVVAPE 238
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRR-RAARPTVGSLTSLADPPPPPPTPEPA 2711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  239 EKTVNPFLPSTPGPKKAKGGGEAVETHPAPGPLPPPEVRDIGERREPDRAQQQ-PQKPAVAAGTQSlGNFRQGFMKCLLE 317
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAA-GPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496216  318 VEKMEASHRRASKARSQTAQKSPRTLTPVPTSAPS--LPQTPASVPASGPSwarLPAPGPEPAPMGAPV 384
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgpLPPPTSAQPTAPPP---PPGPPPPSLPLGGSV 2856
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
448-512 6.62e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 6.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496216 448 QEEAFRSYFEIF--NGPGEVDAQSLKniLLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMTD 512
Cdd:COG5126    67 VEPFARAAFDLLdtDGDGKISADEFR--RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
449-511 1.15e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496216 449 EEAFRSYFEIF--NGPGEVDAQSLKNIL--LLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:pfam13499   1 EEKLKEAFKLLdsDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
 151-426 5.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  151 RGIGEDQPPESCQGSGYQSTPSHQADMVQPAEPccrlashgqPLGGKHPKEAGVPHIRPQEA-PPEPSPGGHGDSSQEAM 229
Cdd:PHA03247   261 VGEGADRAPETARGATGPPPPPEAAAPNGAAAP---------PDGVWGAALAGAPLALPAPPdPPPPAPAGDAEEEDDED 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  230 PPMSVVAPeektvnpflpsTPGPKKAKGGGeaVETHPAPGPLPPPEVRDIGERREPDRAQQQPQKpavaagtqslgnfrq 309
Cdd:PHA03247   332 GAMEVVSP-----------LPRPRQHYPLG--FPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTR--------------- 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  310 gfmkcllevEKMEASHRRASKARSQTAQKSPRTLTPVPTSAPSlpQTPASVPASGPSWARLPAPGPEPAPMGAPVPTSMP 389
Cdd:PHA03247   384 ---------KRRSARHAATPFARGPGGDDQTRPAAPVPASVPT--PAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPER 452

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462496216  390 cpvllGPALDLGWRRMELLHQSSERTLSYAKARQEPE 426
Cdd:PHA03247   453 -----QPPAPATEPAPDDPDDATRKALDALRERRPPE 484
EF-hand_8 pfam13833
EF-hand domain pair;
463-512 2.24e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462496216 463 GEVDAQSLKNILLLMGFS-VTLAQVEDALMSADVNGDGRVDFKDFLAVMTD 512
Cdd:pfam13833   3 GVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 485-511 2.36e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 2.36e-03
                           10        20
                   ....*....|....*....|....*..
gi 2462496216  485 QVEDALMSADVNGDGRVDFKDFLAVMT 511
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
PHA03247 PHA03247
large tegument protein UL36; Provisional
 205-397 2.41e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  205 PHIRPQEAPPEPSPGG-----HG------DSSQEAMPPMSVVAPEEKTVNPFLPSTPGPKKAKGGGEAVETHPAPGPLPP 273
Cdd:PHA03247  2517 PAILPDEPVGEPVHPRmltwiRGleelasDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSA 2596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216  274 PEVRDIGERRE-----------PDRAQQQPQKPAVAAGTQSLGNfRQGFMKCLLEVEKMEASHRRASKARSQTAQKSPrt 342
Cdd:PHA03247  2597 RPRAPVDDRGDprgpappsplpPDTHAPDPPPPSPSPAANEPDP-HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA-- 2673

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462496216  343 ltPVPTSAPSLPQTPASVPASGPSWARLPAPGPEPAPMGAPVPTSMPCPVLLGPA 397
Cdd:PHA03247  2674 --AQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726
PTZ00183 PTZ00183
centrin; Provisional
 456-513 3.14e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.90  E-value: 3.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216 456 FEIF--NGPGEVDAQSLKNILLLMGFSVTLAQVEDALMSADVNGDGRVDFKDFLAVMTDT 513
Cdd:PTZ00183   96 FRLFddDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMKKT 155
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 305-393 3.20e-03

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 38.69  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216 305 GNFRQGFMKCLLEVEkmeashrrASKARSQTAQKSPRTLTPVPTSAPSLPQTPASVPAsgpswarlPAPGPEPAPMGAPV 384
Cdd:PRK05641   23 GKFRVSFEGKTYEVE--------AKGLGIDLSAVQEQVPTPAPAPAPAVPSAPTPVAP--------AAPAPAPASAGENV 86

                          90
                  ....*....|
gi 2462496216 385 PTS-MPCPVL 393
Cdd:PRK05641   87 VTApMPGKIL 96
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 435-511 3.45e-03

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


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 37.51  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496216 435 QNREKSEEQltlkqEEAFRSYFEIFN--GPGEVDAQSLKNILLLMGFSVTLAQVEDA-----LMSADVNGDGRVDFKDFL 507
Cdd:cd16252    27 QKFQTSEQQ-----EEAIRKAFQMLDkdKSGFIEWNEIKYILSTVPSSMPVAPLSDEeaeamIQAADTDGDGRIDFQEFS 101


                  ....
gi 2462496216 508 AVMT 511
Cdd:cd16252   102 DMVK 105
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 486-513 4.82e-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: 35.07  E-value: 4.82e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462496216 486 VEDALMSADVNGDGRVDFKDFLAVMTDT 513
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 330-404 9.69e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 39.16  E-value: 9.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496216 330 KARSQTAQKSPRTLTPVPTSAPSLPQTPASVPASGPSWARLPaPGPEPAPM-GAPVPTSMPCPVLLGPALDLG-WRR 404
Cdd:PRK14954  393 KAPEPDLPQPDRHPGPAKPEAPGARPAELPSPASAPTPEQQP-PVARSAPLpPSPQASAPRNVASGKPGVDLGsWQG 468
 
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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