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Conserved domains on  [gi|334182746|ref|NP_001185056|]
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Calcium-binding EF hand family protein [Arabidopsis thaliana]

Protein Classification

EH domain-containing protein( domain architecture ID 11506103)

EH domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 416-509 2.75e-27

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


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 106.59  E-value: 2.75e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    416 PWPkMTPADVQKYTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYLMERYREG 495
Cdd:smart00027    1 PWA-ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNG 79

                            90
                    ....*....|....
gi 334182746    496 RPLPPVFPSSIIHS 509
Cdd:smart00027   80 YPIPASLPPSLIPP 93
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 13-79 2.35e-23

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: 94.59  E-value: 2.35e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746   13 FDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTVAQS 79
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 635-767 6.95e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   635 VAIVDELEKEIADSKQKIDFFRAKMQELVLYKSRCDNRYNEIAERVLGDKRELESLAKKYEEKYKKSGNVGSKLT-IEea 713
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGdLK-- 888

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 334182746   714 tfRDIQEKKMELYQAIVKFEEGKLDdsiVKRTEHIQSGLEELIKNLNERCKQYG 767
Cdd:TIGR02169  889 --KERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEIE 937
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 95-423 1.45e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    95 PASANIPAPKINLAATPSPQPRGVLPATQAQGVTSMPSVAA-GVRGPH-MGGTVSTSNQQVVPGQQNQFTGI----PPSQ 168
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqSTAAPHtLIQQTPTLHPQRLPSPHPPLQPMtqppPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   169 T------QQNFQSPGMP------AGGTNAPRP-ANQPMPSDWLSGRSVGPSGNVNSQIPSSQSTYGLTAPNSTANH---- 231
Cdd:pfam03154  261 VspqplpQPSLHGQMPPmphslqTGPSHMQHPvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpp 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   232 ---------ITKPHITPAVTSSTTTRPQESAPVHNPQESSATFGSRVSNVPSnqlvPKDPKELAASGNGFTSDSLFGDVF 302
Cdd:pfam03154  341 reqplppapLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPP----PPALKPLSSLSTHHPPSAHPPPLQ 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   303 SVTSTQPKQHPTGSASTTGISSVTTGTVAGPEITQSVvrqSSIPQQGSLSQHAV--GVQTQLTGNSGQPYTSSGAASG-- 378
Cdd:pfam03154  417 LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGL---HQVPSQSPFPQHPFvpGGPPPITPPSGPPTSTSSAMPGiq 493

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 334182746   379 PPGS---TVGVGISATSQLAQRPPHPHSQPQPRPQGQSQPPWPKMTPA 423
Cdd:pfam03154  494 PPSSasvSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPS 541
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 416-509 2.75e-27

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 106.59  E-value: 2.75e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    416 PWPkMTPADVQKYTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYLMERYREG 495
Cdd:smart00027    1 PWA-ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNG 79

                            90
                    ....*....|....
gi 334182746    496 RPLPPVFPSSIIHS 509
Cdd:smart00027   80 YPIPASLPPSLIPP 93
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 13-79 2.35e-23

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: 94.59  E-value: 2.35e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746   13 FDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTVAQS 79
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 428-494 8.43e-23

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: 93.05  E-value: 8.43e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746  428 YTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYLMERYRE 494
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 6-87 8.52e-16

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 73.85  E-value: 8.52e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746      6 PTGGQDLFDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTVAQSRRELTA 85
Cdd:smart00027    5 SPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPA 84


                    ..
gi 334182746     86 EI 87
Cdd:smart00027   85 SL 86
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 418-488 6.34e-12

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 63.16  E-value: 6.34e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182746   418 PKMTPADVQKYTKVFvQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYL 488
Cdd:pfam12763    2 PRLEEWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRL 71
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
420-486 1.39e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 1.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746  420 MTPADVQKYTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAV 486
Cdd:COG5126    63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-72 9.05e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 9.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182746    1 MAAPRPTGGQDLFDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALK 72
Cdd:COG5126    59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
17-72 3.83e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 3.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    17 FRRADLDGDGHISGAEAVAFFQ----GSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALK 72
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 635-767 6.95e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   635 VAIVDELEKEIADSKQKIDFFRAKMQELVLYKSRCDNRYNEIAERVLGDKRELESLAKKYEEKYKKSGNVGSKLT-IEea 713
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGdLK-- 888

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 334182746   714 tfRDIQEKKMELYQAIVKFEEGKLDdsiVKRTEHIQSGLEELIKNLNERCKQYG 767
Cdd:TIGR02169  889 --KERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEIE 937
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 95-423 1.45e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    95 PASANIPAPKINLAATPSPQPRGVLPATQAQGVTSMPSVAA-GVRGPH-MGGTVSTSNQQVVPGQQNQFTGI----PPSQ 168
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqSTAAPHtLIQQTPTLHPQRLPSPHPPLQPMtqppPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   169 T------QQNFQSPGMP------AGGTNAPRP-ANQPMPSDWLSGRSVGPSGNVNSQIPSSQSTYGLTAPNSTANH---- 231
Cdd:pfam03154  261 VspqplpQPSLHGQMPPmphslqTGPSHMQHPvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpp 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   232 ---------ITKPHITPAVTSSTTTRPQESAPVHNPQESSATFGSRVSNVPSnqlvPKDPKELAASGNGFTSDSLFGDVF 302
Cdd:pfam03154  341 reqplppapLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPP----PPALKPLSSLSTHHPPSAHPPPLQ 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   303 SVTSTQPKQHPTGSASTTGISSVTTGTVAGPEITQSVvrqSSIPQQGSLSQHAV--GVQTQLTGNSGQPYTSSGAASG-- 378
Cdd:pfam03154  417 LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGL---HQVPSQSPFPQHPFvpGGPPPITPPSGPPTSTSSAMPGiq 493

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 334182746   379 PPGS---TVGVGISATSQLAQRPPHPHSQPQPRPQGQSQPPWPKMTPA 423
Cdd:pfam03154  494 PPSSasvSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPS 541
PHA03247 PHA03247
large tegument protein UL36; Provisional
 94-426 2.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   94 SPASANIPAPKINLAATPSPQPRGVLPATQAQGVTSMPSVAAGVRGPhmgGTVSTSNQQVVPGQQNQftgipPSQTQQNF 173
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP---GRVSRPRRARRLGRAAQ-----ASSPPQRP 2683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  174 QSPGMPA--------GGTNAPRPANQPMPSDWLSGrsvgpsgnvnSQIPSSQSTYGLTAPNSTANHITKPHITPAVTSST 245
Cdd:PHA03247 2684 RRRAARPtvgsltslADPPPPPPTPEPAPHALVSA----------TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  246 TTRPQESAPVHNPQESSATFGSrvSNVPSNQLVPKDPKELAASGNGFTSDSLFGDVFSVTSTQPKQHPTGSASTTGISSV 325
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAP--AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  326 TTGTVAGPEITQSVVrQSSIPQQGSLsqhAVGVQTQLTGNSGQPYTSSGAASGPPGSTVGVGI--SATSQLAQRPPHPHS 403
Cdd:PHA03247 2832 TSAQPTAPPPPPGPP-PPSLPLGGSV---APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvsRSTESFALPPDQPER 2907

                         330       340
                  ....*....|....*....|...
gi 334182746  404 QPQPRPQGQSQPPWPKMTPADVQ 426
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQ 2930
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 416-509 2.75e-27

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 106.59  E-value: 2.75e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    416 PWPkMTPADVQKYTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYLMERYREG 495
Cdd:smart00027    1 PWA-ISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNG 79

                            90
                    ....*....|....
gi 334182746    496 RPLPPVFPSSIIHS 509
Cdd:smart00027   80 YPIPASLPPSLIPP 93
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 13-79 2.35e-23

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: 94.59  E-value: 2.35e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746   13 FDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTVAQS 79
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 428-494 8.43e-23

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: 93.05  E-value: 8.43e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746  428 YTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYLMERYRE 494
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 6-87 8.52e-16

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 73.85  E-value: 8.52e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746      6 PTGGQDLFDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTVAQSRRELTA 85
Cdd:smart00027    5 SPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPA 84


                    ..
gi 334182746     86 EI 87
Cdd:smart00027   85 SL 86
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 418-488 6.34e-12

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 63.16  E-value: 6.34e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182746   418 PKMTPADVQKYTKVFvQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAVYL 488
Cdd:pfam12763    2 PRLEEWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRL 71
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
420-486 1.39e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 1.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182746  420 MTPADVQKYTKVFVQVDTDRDGKITGNQARNLFLSWRLPRDALKQVWDLSDQDNDSMLSLREFCIAV 486
Cdd:COG5126    63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-72 9.05e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 9.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182746    1 MAAPRPTGGQDLFDTYFRRADLDGDGHISGAEAVAFFQGSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALK 72
Cdd:COG5126    59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
431-487 2.32e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 2.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182746   431 VFVQVDTDRDGKITGNQARNLFLSWR----LPRDALKQVWDLSDQDNDSMLSLREFCIAVY 487
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEegepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 13-83 2.45e-04

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 42.27  E-value: 2.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182746   13 FDTYFRRADLDGDGHISGAEAVAFFQGSN--LPKHVLAQVWSYADSKKAGYLGRAEFYNALKLVTvaqSRREL 83
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNirVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT---ERPEL 71
EF-hand_7 pfam13499
EF-hand domain pair;
17-72 3.83e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 3.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    17 FRRADLDGDGHISGAEAVAFFQ----GSNLPKHVLAQVWSYADSKKAGYLGRAEFYNALK 72
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 427-483 4.39e-04

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: 39.45  E-value: 4.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 334182746  427 KYTKVFVQVDTDRDGKITGNQARNLF--LSWRLPRDALKQVWDLSDQDNDSMLSLREFC 483
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 635-767 6.95e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   635 VAIVDELEKEIADSKQKIDFFRAKMQELVLYKSRCDNRYNEIAERVLGDKRELESLAKKYEEKYKKSGNVGSKLT-IEea 713
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGdLK-- 888

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 334182746   714 tfRDIQEKKMELYQAIVKFEEGKLDdsiVKRTEHIQSGLEELIKNLNERCKQYG 767
Cdd:TIGR02169  889 --KERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEIE 937
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 95-423 1.45e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    95 PASANIPAPKINLAATPSPQPRGVLPATQAQGVTSMPSVAA-GVRGPH-MGGTVSTSNQQVVPGQQNQFTGI----PPSQ 168
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqSTAAPHtLIQQTPTLHPQRLPSPHPPLQPMtqppPPSQ 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   169 T------QQNFQSPGMP------AGGTNAPRP-ANQPMPSDWLSGRSVGPSGNVNSQIPSSQSTYGLTAPNSTANH---- 231
Cdd:pfam03154  261 VspqplpQPSLHGQMPPmphslqTGPSHMQHPvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpp 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   232 ---------ITKPHITPAVTSSTTTRPQESAPVHNPQESSATFGSRVSNVPSnqlvPKDPKELAASGNGFTSDSLFGDVF 302
Cdd:pfam03154  341 reqplppapLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPP----PPALKPLSSLSTHHPPSAHPPPLQ 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   303 SVTSTQPKQHPTGSASTTGISSVTTGTVAGPEITQSVvrqSSIPQQGSLSQHAV--GVQTQLTGNSGQPYTSSGAASG-- 378
Cdd:pfam03154  417 LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGL---HQVPSQSPFPQHPFvpGGPPPITPPSGPPTSTSSAMPGiq 493

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 334182746   379 PPGS---TVGVGISATSQLAQRPPHPHSQPQPRPQGQSQPPWPKMTPA 423
Cdd:pfam03154  494 PPSSasvSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPS 541
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 63-392 1.92e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 42.25  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746    63 GRAEFYNALKLVTVAQSRRELTAEIVKAAIYSPASANIPAPKINLAATP-SPQPRGVLPATQAQGVTSMPSVAAGVRGPH 141
Cdd:pfam17823  105 GAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANaSAAPRAAIAAASAPHAASPAPRTAASSTTA 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   142 MGGTVSTSNQQVVPGQQNQFTGIPPSQTQQNFQSPGMPAGGT-NAPRPANQPMP-SDWLSGRSVGPS--GNVNSQIPSSQ 217
Cdd:pfam17823  185 ASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTaLAAVGNSSPAAgTVTAAVGTVTPAalATLAAAAGTVA 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   218 STYGltAPNSTANHITKPhiTPAVTSSTTTRPQESAPVHNPQESSATfgsrvSNVPSNQLVPKDPKELAASGngftsdsl 297
Cdd:pfam17823  265 SAAG--TINMGDPHARRL--SPAKHMPSDTMARNPAAPMGAQAQGPI-----IQVSTDQPVHNTAGEPTPSP-------- 327

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   298 fgdvfsvTSTQPKQHPTGSASTTGISSVTTGTVAGPEITQS---VVRQSSIPQqgslsqhaVGVQTQLTGNSGQPYTSSG 374
Cdd:pfam17823  328 -------SNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASpvpVLHTSMIPE--------VEATSPTTQPSPLLPTQGA 392

                          330
                   ....*....|....*...
gi 334182746   375 AASGPPGSTVGVGISATS 392
Cdd:pfam17823  393 AGPGILLAPEQVATEATA 410
PHA03247 PHA03247
large tegument protein UL36; Provisional
 94-426 2.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   94 SPASANIPAPKINLAATPSPQPRGVLPATQAQGVTSMPSVAAGVRGPhmgGTVSTSNQQVVPGQQNQftgipPSQTQQNF 173
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP---GRVSRPRRARRLGRAAQ-----ASSPPQRP 2683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  174 QSPGMPA--------GGTNAPRPANQPMPSDWLSGrsvgpsgnvnSQIPSSQSTYGLTAPNSTANHITKPHITPAVTSST 245
Cdd:PHA03247 2684 RRRAARPtvgsltslADPPPPPPTPEPAPHALVSA----------TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  246 TTRPQESAPVHNPQESSATFGSrvSNVPSNQLVPKDPKELAASGNGFTSDSLFGDVFSVTSTQPKQHPTGSASTTGISSV 325
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAP--AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  326 TTGTVAGPEITQSVVrQSSIPQQGSLsqhAVGVQTQLTGNSGQPYTSSGAASGPPGSTVGVGI--SATSQLAQRPPHPHS 403
Cdd:PHA03247 2832 TSAQPTAPPPPPGPP-PPSLPLGGSV---APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvsRSTESFALPPDQPER 2907

                         330       340
                  ....*....|....*....|...
gi 334182746  404 QPQPRPQGQSQPPWPKMTPADVQ 426
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQ 2930
PHA03247 PHA03247
large tegument protein UL36; Provisional
 88-356 5.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746   88 VKAAIYSPASANIPAPKINLAATPSPQPRGVlPATQAQGVTSMPSVAAGV---------RGPHMGGTVSTSNQQVVPGQQ 158
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSesreslpspWDPADPPAAVLAPAAALPPAA 2822

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  159 NQFTGIPPSQTQQnfqspgmPAggtnAPRPANQPMPSDWLSGRSVGPSGNVNSQIPSSQSTYGLTAPnstanhiTKPHIT 238
Cdd:PHA03247 2823 SPAGPLPPPTSAQ-------PT----APPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP-------ARPPVR 2884

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182746  239 ----PAVTSSTTTRPQESAPVHNPQESSATFGSRVSNVPSNQLVPKDPKELAASGNGFTSDSlfgdvfsvTSTQPKQHPT 314
Cdd:PHA03247 2885 rlarPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT--------TDPAGAGEPS 2956

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 334182746  315 GSASTTGISSVTTGTVAGPEITQSVVRQS---SIPQQGSLSQHAV 356
Cdd:PHA03247 2957 GAVPQPWLGALVPGRVAVPRFRVPQPAPSreaPASSTPPLTGHSL 3001
 
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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