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Conserved domains on  [gi|14249254|ref|NP_116069|]
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EF-hand calcium-binding domain-containing protein 4B isoform c [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-118 1.11e-07

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  35 SLEQKETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELEDVFDALDADGNGYLTPQEFTTGFS 114
Cdd:COG5126  51 SREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130


                ....
gi 14249254 115 HFFF 118
Cdd:COG5126 131 DYYT 134
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-370 4.67e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    201 LTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHLYE-----EMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQ 275
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    276 ELEQLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVt 355
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR- 416

                          170
                   ....*....|....*
gi 14249254    356 ESLQREKAGLLKQLD 370
Cdd:TIGR02168  417 ERLQQEIEELLKKLE 431
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-118 1.11e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  35 SLEQKETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELEDVFDALDADGNGYLTPQEFTTGFS 114
Cdd:COG5126  51 SREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130


                ....
gi 14249254 115 HFFF 118
Cdd:COG5126 131 DYYT 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-370 4.67e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    201 LTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHLYE-----EMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQ 275
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    276 ELEQLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVt 355
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR- 416

                          170
                   ....*....|....*
gi 14249254    356 ESLQREKAGLLKQLD 370
Cdd:TIGR02168  417 ERLQQEIEELLKKLE 431
PRK12704 PRK12704
phosphodiesterase; Provisional
 213-323 1.75e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  213 EEKNELECALKRKIAAYDEEIQHLYEEMEQQIKSEKEQFllkdterfqarsQELEQKLLCKEQ----ELEQLTQKQKRLE 288
Cdd:PRK12704  46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNEL------------QKLEKRLLQKEEnldrKLELLEKREEELE 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14249254  289 GQCTALHHDKHETKAENTKLKLTNQELARELERTS 323
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
PRK12309 PRK12309
transaldolase;
33-113 3.25e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.49  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   33 LDSLEQ--KETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMqrlhkelplslEELEDVFDALDADGNGYLTPQEFT 110
Cdd:PRK12309 312 LETLEKllAHRLARLEGGEAFTHAAQEIFRLYDLDGDGFITREEW-----------LGSDAVFDALDLNHDGKITPEEMR 380


                 ...
gi 14249254  111 TGF 113
Cdd:PRK12309 381 AGL 383
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 188-373 1.42e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   188 KEEPHLLSNFEDFLTRIISQLQEAHEEKNELE---CALKRKIAAYDEEIQHL---YEEMEQQIK---------SEKEQFL 252
Cdd:pfam07888  41 QERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSrekHEELEEKYKelsasseelSEEKDAL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   253 LKDTERFQARSQELE-------QKLLCKEQELEQLTQKQKRLEGQctalhhdKHETKAENTKLKLTNQELARELERTSWE 325
Cdd:pfam07888 121 LAQRAAHEARIRELEediktltQRVLERETELERMKERAKKAGAQ-------RKEEEAERKQLQAKLQQTEEELRSLSKE 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 14249254   326 LQDAQQQLESLQQEACKLHQEKEMEVYRVTESLQREKA--GLLKQLDFLR 373
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneALLEELRSLQ 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 185-321 2.17e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 185 QLKKEEPHLLSNFEDFLTRIISQLQEAHEEKNELEcalkRKIAAYDEEIQHL------YEEMEQQIKSEKE-QFLLKDTE 257
Cdd:COG1579  24 HRLKELPAELAELEDELAALEARLEAAKTELEDLE----KEIKRLELEIEEVearikkYEEQLGNVRNNKEyEALQKEIE 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14249254 258 RFQARSQELEQKLLCKEQELEQLTQKQKRLEGQCTALHHDKHETKAE-NTKLKLTNQELARELER 321
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAElDEELAELEAELEELEAE 164
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 54-114 2.76e-03

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: 35.99  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14249254  54 KAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELE--DVFDALDADGNGYLTPQEFTTGFS 114
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEidEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
54-114 3.18e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14249254    54 KAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELED----VFDALDADGNGYLTPQEFTTGFS 114
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEeveeLFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-118 1.11e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  35 SLEQKETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELEDVFDALDADGNGYLTPQEFTTGFS 114
Cdd:COG5126  51 SREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130


                ....
gi 14249254 115 HFFF 118
Cdd:COG5126 131 DYYT 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-370 4.67e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    201 LTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHLYE-----EMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQ 275
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    276 ELEQLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVt 355
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR- 416

                          170
                   ....*....|....*
gi 14249254    356 ESLQREKAGLLKQLD 370
Cdd:TIGR02168  417 ERLQQEIEELLKKLE 431
PRK12704 PRK12704
phosphodiesterase; Provisional
 213-323 1.75e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  213 EEKNELECALKRKIAAYDEEIQHLYEEMEQQIKSEKEQFllkdterfqarsQELEQKLLCKEQ----ELEQLTQKQKRLE 288
Cdd:PRK12704  46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNEL------------QKLEKRLLQKEEnldrKLELLEKREEELE 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14249254  289 GQCTALHHDKHETKAENTKLKLTNQELARELERTS 323
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
PRK12309 PRK12309
transaldolase;
33-113 3.25e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 45.49  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   33 LDSLEQ--KETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMqrlhkelplslEELEDVFDALDADGNGYLTPQEFT 110
Cdd:PRK12309 312 LETLEKllAHRLARLEGGEAFTHAAQEIFRLYDLDGDGFITREEW-----------LGSDAVFDALDLNHDGKITPEEMR 380


                 ...
gi 14249254  111 TGF 113
Cdd:PRK12309 381 AGL 383
PRK12704 PRK12704
phosphodiesterase; Provisional
 223-368 6.93e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  223 KRKIAAYDEEIQHLYEEMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQELEQ----LTQKQKRLEGQCTALhhDK 298
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELL--EK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249254  299 HETKAENTKLKLTNQElaRELERTSWELQDAQQQLESLQQEACKLHQE--KEMEVYRVTESLQREKAGLLKQ 368
Cdd:PRK12704 108 REEELEKKEKELEQKQ--QELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAVLIKE 177
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
48-134 2.44e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  48 QLVMLRKAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEEL--EDVFDALDADGNGYLTPQEFTTgfshfFFSQNNPSQ 125
Cdd:COG5126  28 EALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPfaRAAFDLLDTDGDGKISADEFRR-----LLTALGVSE 102


                ....*....
gi 14249254 126 EDAGEQVAQ 134
Cdd:COG5126 103 EEADELFAR 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-365 7.01e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 7.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    170 QKVLEDESDVKQLWLQLKKEEPHLLSNFEDFLTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHL---YEEMEQQIKS 246
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIAS 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    247 EKEQFllkdtERFQARSQELEQKLLCKEQELEQLTQKQKRLEGQctALHHDKHETKAENTKLKLTNQELARELERTSWEL 326
Cdd:TIGR02168  398 LNNEI-----ERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREEL 470

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 14249254    327 QDAQQQLESLQQEACKLHQEKEMevyrvTESLQREKAGL 365
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDS-----LERLQENLEGF 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-370 9.32e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    185 QLKKEEPHLLSNFEDFLTRIISQLQEAHEEKNELEcALKRKIAAYDEEIQHLYEEMEQQIKSEKEQfllkdterfQARSQ 264
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKELTELEAEIEEL---------EERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254    265 ELEQKLLCKEQELEQLTQKQKRLEGQCT-------ALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQ 337
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851

                          170       180       190
                   ....*....|....*....|....*....|...
gi 14249254    338 QEACKLHQEKEMEVYRVTEsLQREKAGLLKQLD 370
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEE-LESELEALLNERA 883
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 188-373 1.42e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   188 KEEPHLLSNFEDFLTRIISQLQEAHEEKNELE---CALKRKIAAYDEEIQHL---YEEMEQQIK---------SEKEQFL 252
Cdd:pfam07888  41 QERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSrekHEELEEKYKelsasseelSEEKDAL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   253 LKDTERFQARSQELE-------QKLLCKEQELEQLTQKQKRLEGQctalhhdKHETKAENTKLKLTNQELARELERTSWE 325
Cdd:pfam07888 121 LAQRAAHEARIRELEediktltQRVLERETELERMKERAKKAGAQ-------RKEEEAERKQLQAKLQQTEEELRSLSKE 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 14249254   326 LQDAQQQLESLQQEACKLHQEKEMEVYRVTESLQREKA--GLLKQLDFLR 373
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneALLEELRSLQ 243
PRK00106 PRK00106
ribonuclease Y;
230-366 1.89e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254  230 DEEIQHLYEEMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQELEQLtqkQKRLEGQCTALhhdkhETKAENtklk 309
Cdd:PRK00106  52 ERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQI---ESRLTERATSL-----DRKDEN---- 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14249254  310 LTNQELAreLERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVTESLQREKAGLL 366
Cdd:PRK00106 120 LSSKEKT--LESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREII 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 185-321 2.17e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 185 QLKKEEPHLLSNFEDFLTRIISQLQEAHEEKNELEcalkRKIAAYDEEIQHL------YEEMEQQIKSEKE-QFLLKDTE 257
Cdd:COG1579  24 HRLKELPAELAELEDELAALEARLEAAKTELEDLE----KEIKRLELEIEEVearikkYEEQLGNVRNNKEyEALQKEIE 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14249254 258 RFQARSQELEQKLLCKEQELEQLTQKQKRLEGQCTALHHDKHETKAE-NTKLKLTNQELARELER 321
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAElDEELAELEAELEELEAE 164
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 54-114 2.76e-03

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: 35.99  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14249254  54 KAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELE--DVFDALDADGNGYLTPQEFTTGFS 114
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEidEMIREVDKDGDGKIDFEEFLELMA 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-353 3.01e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 201 LTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHLYEEMEQQIKSEKEQF-LLKDTERFQARSQELEQKLLCKEQELEQ 279
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLER 418

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14249254 280 LTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYR 353
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
EF-hand_7 pfam13499
EF-hand domain pair;
54-114 3.18e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14249254    54 KAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELED----VFDALDADGNGYLTPQEFTTGFS 114
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEeveeLFKEFDLDKDGRISFEEFLELYS 67
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 205-283 4.13e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.02  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   205 ISQLQEAHEEKNELECALKRKIaayDEEIQHLYEEME------QQIKSEKEQFLLKDTERFQARS---QELEQKLLCKEQ 275
Cdd:pfam15905 245 IAQLEELLKEKNDEIESLKQSL---EEKEQELSKQIKdlnekcKLLESEKEELLREYEEKEQTLNaelEELKEKLTLEEQ 321


                  ....*...
gi 14249254   276 ELEQLTQK 283
Cdd:pfam15905 322 EHQKLQQK 329
DUF445 pfam04286
Protein of unknown function (DUF445); Predicted to be a membrane protein.
 145-289 4.62e-03

Protein of unknown function (DUF445); Predicted to be a membrane protein.


Pssm-ID: 427840 [Multi-domain]  Cd Length: 368  Bit Score: 38.76  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254   145 GDEDLGDMGED--EEAQFRMLMDRLGAQKVLEDESDvkqlWLQLKKEEP-HLLSN-FEDFLTRIISQLQEAHEEKNELEc 220
Cdd:pfam04286 159 GKQRIAEMIDEflEEWGPLVALLGGIAEMILRALSS----LLDEVQADPdHPLRLaFDRAVRELITDLLNDPELRAEVE- 233

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14249254   221 ALKRKIAAyDEEIQHLYEEMEQQIKSEKEQFLLKDTERFQARSQELEQKLlckEQELEQLTQKQKRLEG 289
Cdd:pfam04286 234 ELKQKLLA-DPAVQDYVKALWESLRSLLLDDLSDPDSALRRRISELLAEF---GERLAEDPELRDKLNE 298
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 164-373 5.36e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 164 MDRLGAQ-------KVLEDESDVKQLWLQLKKeephllsnfedfLTRIISQLQEAHEEKNELECALKRKIAAYdEEIQHL 236
Cdd:COG1196 202 LEPLERQaekaeryRELKEELKELEAELLLLK------------LRELEAELEELEAELEELEAELEELEAEL-AELEAE 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 237 YEEMEQQIksekeqfllkdtERFQARSQELEQKLLCKEQELEQLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELA 316
Cdd:COG1196 269 LEELRLEL------------EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14249254 317 RELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVTESLQREKAGLLKQLDFLR 373
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-373 6.60e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 205 ISQLQEAHEEKNELECALKRKIAAYDEEIQHLyEEMEQQIKSEKEQF------LLKDTERFQARSQELEQKLLCKEQELE 278
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELeeelaeLEEELEELEEELEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249254 279 QLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVTESL 358
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                       170
                ....*....|....*
gi 14249254 359 QREKAGLLKQLDFLR 373
Cdd:COG1196 435 EEEEEEEEALEEAAE 449
 
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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