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Conserved domains on  [gi|281362966|ref|NP_610466|]
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Rad51 recombinase D [Drosophila melanogaster]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 94-300 1.98e-40

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19489:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 209  Bit Score: 140.85  E-value: 1.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  94 QPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAAT 173
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 174 GADINDLLKSFDHQL-TAETHASMQTKLVLIDSLAACFAFYRGRRMRDVRKSVLTELACKIRKLALR-GVAFVIGNVSFf 251
Cdd:cd19489   82 PYELLDLLEELRNTLsQQQENLYSRLKLVIIDSLSALISPLLGGSKHSEGHALLASLARLLKKLAAEyQIAVLVTNLTV- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 281362966 252 ennkdscgddgeqnGDDEEVTRQQLEPMLGSYWSSVATLRLSVELPEEE 300
Cdd:cd19489  161 --------------RGGDGGQQGSTKPALGEYWESVPSTRLLLSRDEND 195
 
Name Accession Description Interval E-value
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 94-300 1.98e-40

RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410897 [Multi-domain]  Cd Length: 209  Bit Score: 140.85  E-value: 1.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  94 QPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAAT 173
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 174 GADINDLLKSFDHQL-TAETHASMQTKLVLIDSLAACFAFYRGRRMRDVRKSVLTELACKIRKLALR-GVAFVIGNVSFf 251
Cdd:cd19489   82 PYELLDLLEELRNTLsQQQENLYSRLKLVIIDSLSALISPLLGGSKHSEGHALLASLARLLKKLAAEyQIAVLVTNLTV- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 281362966 252 ennkdscgddgeqnGDDEEVTRQQLEPMLGSYWSSVATLRLSVELPEEE 300
Cdd:cd19489  161 --------------RGGDGGQQGSTKPALGEYWESVPSTRLLLSRDEND 195
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 80-335 4.32e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 61.80  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLALNFVwKHSQAVLFIDTkrE-FSCKRIQDMlrAREVDEEA 158
Cdd:PRK09361   7 TGCKMLDELLGG---GFERGTITQIYGPPGSGKTNICLQLAVEAA-KNGKKVIYIDT--EgLSPERFKQI--AGEDFEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 159 SERamkgIRVVQAatgadindllKSFDHQLTA----ETHASMQTKLVLIDSLAacfAFYR---------GRRMRDVRK-- 223
Cdd:PRK09361  79 LSN----IIIFEP----------SSFEEQSEAirkaEKLAKENVGLIVLDSAT---SLYRleledeednSKLNRELGRql 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 224 SVLTELAckiRKlalRGVAFVIGNVSFFENNKDScgddgeqngddeevtrqqLEPMLGS---YWSSvATLRLsvelpeeE 300
Cdd:PRK09361 142 THLLKLA---RK---HDLAVVITNQVYSDIDSDG------------------LRPLGGHtleHWSK-TILRL-------E 189

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 281362966 301 DFTlqdDGLRFIYVISNTYGPDGEHCLLRITDAGV 335
Cdd:PRK09361 190 KFR---NGKRRATLEKHRSRPEGESAEFRITDRGI 221
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 80-247 9.29e-10

Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.


Pssm-ID: 462471 [Multi-domain]  Cd Length: 255  Bit Score: 58.47  E-value: 9.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966   80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQ-----AVLFIDTKREFSCKRIQDMLRAREV 154
Cdd:pfam08423  21 TGSKELDKLLGG---GIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMgggegKALYIDTEGTFRPERLVAIAERYGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  155 DEEAserAMKGIRVVQAATGADINDLLksfdhQLTAETHASMQTKLVLIDSLAACF-AFYRGRRMRDVRKSVLTELACKI 233
Cdd:pfam08423  98 DPED---VLDNVAYARAYNSEHQMQLL-----QQAAAMMSESRFALLIVDSATALYrTDFSGRGELAERQQHLAKFLRTL 169

                         170
                  ....*....|....*
gi 281362966  234 RKLALR-GVAFVIGN 247
Cdd:pfam08423 170 QRLADEfGVAVVITN 184
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
80-241 1.66e-05

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 45.29  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLdsvEQPFKPGRVWELCGQPGVGKTqllyTLALNFVW---KHSQAVLFIDTkrEFSCKRIQDMLRAREVDE 156
Cdd:COG0467    4 TGIPGLDELL---GGGLPRGSSTLLSGPPGTGKT----TLALQFLAeglRRGEKGLYVSF--EESPEQLLRRAESLGLDL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 157 EASERAMKgIRVVQAATGADINDlLKSFDHQLtAETHASMQTKLVLIDSLAACFAFYRGRRMrdvRKSVLTELackIRKL 236
Cdd:COG0467   75 EEYIESGL-LRIIDLSPEELGLD-LEELLARL-REAVEEFGAKRVVIDSLSGLLLALPDPER---LREFLHRL---LRYL 145


                 ....*
gi 281362966 237 ALRGV 241
Cdd:COG0467  146 KKRGV 150
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
 80-237 7.23e-04

meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.


Pssm-ID: 131292 [Multi-domain]  Cd Length: 313  Bit Score: 40.92  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966   80 TGIEELDKLLDSVEQPFKpgrVWELCGQPGVGKTQLLYTLALNFVWKHSQA-----VLFIDTKREFSCKRIQDMLRAREV 154
Cdd:TIGR02238  80 TGSQALDGILGGGIESMS---ITEVFGEFRCGKTQLSHTLCVTAQLPREMGggngkVAYIDTEGTFRPDRIRAIAERFGV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  155 DEEAserAMKGIRVVQAATGADINDLLKsfdhQLTAETHaSMQTKLVLIDSLAACFAF-YRGRRMRDVRKSVLTELACKI 233
Cdd:TIGR02238 157 DPDA---VLDNILYARAYTSEHQMELLD----YLAAKFS-EEPFRLLIVDSIMALFRVdFSGRGELSERQQKLAQMLSRL 228


                  ....
gi 281362966  234 RKLA 237
Cdd:TIGR02238 229 NKIS 232
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 98-172 7.56e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 7.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362966    98 PGRVWELCGQPGVGKTQLLYTLALNFVwKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAA 172
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
 
Name Accession Description Interval E-value
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 94-300 1.98e-40

RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410897 [Multi-domain]  Cd Length: 209  Bit Score: 140.85  E-value: 1.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  94 QPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAAT 173
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 174 GADINDLLKSFDHQL-TAETHASMQTKLVLIDSLAACFAFYRGRRMRDVRKSVLTELACKIRKLALR-GVAFVIGNVSFf 251
Cdd:cd19489   82 PYELLDLLEELRNTLsQQQENLYSRLKLVIIDSLSALISPLLGGSKHSEGHALLASLARLLKKLAAEyQIAVLVTNLTV- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 281362966 252 ennkdscgddgeqnGDDEEVTRQQLEPMLGSYWSSVATLRLSVELPEEE 300
Cdd:cd19489  161 --------------RGGDGGQQGSTKPALGEYWESVPSTRLLLSRDEND 195
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 99-292 2.67e-16

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 75.85  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  99 GRVWELCGQPGVGKTQLLYTLALNfVWKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAATGadin 178
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAAN-ALLLGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPDT---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 179 dllksfDHQLTAETHA------SMQTKLVLIDSLAACFAFYRGRRMRDV-----RKSVLTELACKIRKLA-LRGVAFVIG 246
Cdd:cd01393   76 ------LAHLLALDSLpeslfpPPNTSLVVVDSVSALFRKAFPRGGDGDsssslRARLLSQLARALQKLAaQFNLAVVVT 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281362966 247 NvsffennkdSCGDDGEQNGDDEEVTrqqlePMLGSYWSSVATLRL 292
Cdd:cd01393  150 N---------QVTTKIRGGSGASLVP-----PALGNTWEHSVSTRL 181
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
 96-294 3.14e-16

XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410899 [Multi-domain]  Cd Length: 250  Bit Score: 76.95  E-value: 3.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  96 FKPGRVWELCGQPGVGKTQLLYTLALNFVWKHS-----QAVLFIDTKREFSCKRIQDMLRARE--VDEEASERAMKGIRV 168
Cdd:cd19491    9 IPVGGITEIAGESGAGKTQLCLQLALTVQLPRElgglgGGAVYICTESSFPSKRLQQLASSLPkrYHLEKAKNFLDNIFV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 169 VQAatgADINDLLKSFDHQLTA--ETHasmQTKLVLIDSLAACFAFYRGRRMRDV--RKSVLTELACKIRKLALR-GVAF 243
Cdd:cd19491   89 EHV---ADLETLEHCLNYQLPAllERG---PIRLVVIDSIAALFRSEFDTSRSDLveRAKYLRRLADHLKRLADKyNLAV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 281362966 244 VIGN-VS--FFENNKDSCGDDGEQ----NGDDEEVTRQQLEPMLGSYWSSVATLRLSV 294
Cdd:cd19491  163 VVVNqVTdrFDSSSDASGLGVLDYlsqfSSFSGGVSGNRKVPALGLTWANLVNTRLML 220
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 99-292 9.06e-14

RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.


Pssm-ID: 410900 [Multi-domain]  Cd Length: 172  Bit Score: 68.40  E-value: 9.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  99 GRVWELCGQPGVGKTQLLYTLALNfVWKHSQA------VLFIDTKREFsckRIQdMLRAREVDEeaseramkgirvvQAA 172
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVN-VQIPKCFgglageAIYIDTEGSF---NIH-YFRVHDYVE-------------LLA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 173 TgadINdLLKSF--DHQltaethasmQTKLVLIDSLAacFAFYRGRRMRDVRKSVLTELACKIRKLALR-GVAFVIGN-V 248
Cdd:cd19492   63 L---IN-SLPKFleDHP---------KVKLIVVDSIA--FPFRHDFDDLAQRTRLLNGLAQLLHSLARQhNLAVVLTNqV 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281362966 249 SF-FENNKDScgddgeqngddeevtrqQLEPMLGSYWSSVATLRL 292
Cdd:cd19492  128 TTkISEDGQS-----------------QLVPALGESWSHACTTRL 155
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 99-295 6.24e-13

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 66.96  E-value: 6.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  99 GRVWELCGQPGVGKTQLLYTLA-----------LNFVwkhsqaVLFIDTKREFSCKRIQDMLRAR--------EVDEEAS 159
Cdd:cd19493   11 GAITEITGASGSGKTQFALTLAssaamparkggLDGG------VLYIDTESKFSAERLAEIAEARfpeafsgfMEENERA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 160 ERAMKGIRVVqaaTGADINDLLKSFDHqlTAETHASMQTKLVLIDSLAACFafyrGRRMRDV------RKSVLTELACKI 233
Cdd:cd19493   85 EEMLKRVAVV---RVTTLAQLLERLPN--LEEHILSSGVRLVVIDSIAALV----RREFGGSdgevteRHNALAREASSL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362966 234 RKLA--LRgVAFVIGNVSFFENNkdscgddgeqngdDEEVTRQQLEPMLGSYWSSVATLRLSVE 295
Cdd:cd19493  156 KRLAeeFR-IAVLVTNQATTHFG-------------DAGDGSSGVTAALGDAWAHAVNTRLRLE 205
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 80-335 4.32e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 61.80  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLALNFVwKHSQAVLFIDTkrE-FSCKRIQDMlrAREVDEEA 158
Cdd:PRK09361   7 TGCKMLDELLGG---GFERGTITQIYGPPGSGKTNICLQLAVEAA-KNGKKVIYIDT--EgLSPERFKQI--AGEDFEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 159 SERamkgIRVVQAatgadindllKSFDHQLTA----ETHASMQTKLVLIDSLAacfAFYR---------GRRMRDVRK-- 223
Cdd:PRK09361  79 LSN----IIIFEP----------SSFEEQSEAirkaEKLAKENVGLIVLDSAT---SLYRleledeednSKLNRELGRql 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 224 SVLTELAckiRKlalRGVAFVIGNVSFFENNKDScgddgeqngddeevtrqqLEPMLGS---YWSSvATLRLsvelpeeE 300
Cdd:PRK09361 142 THLLKLA---RK---HDLAVVITNQVYSDIDSDG------------------LRPLGGHtleHWSK-TILRL-------E 189

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 281362966 301 DFTlqdDGLRFIYVISNTYGPDGEHCLLRITDAGV 335
Cdd:PRK09361 190 KFR---NGKRRATLEKHRSRPEGESAEFRITDRGI 221
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 80-335 7.35e-11

archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 61.18  E-value: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVlFIDTKrEFSCKRIQDMLRARevdeeaS 159
Cdd:cd01394    3 TGSKSLDSLLGG---GVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVV-YIDTE-GLSPERFQQIAGER------F 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 160 ERAMKGIRVVQAatgadindllKSFDHQLTA--ETHA---SMQTKLVLIDSLAAcfaFYRGRRMRDvrKSVLTELACKIR 234
Cdd:cd01394   72 ESIASNIIVFEP----------YSFDEQGVAiqEAEKllkSDKVDLVVVDSATA---LYRLELGDD--SEANRELSRQMS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 235 KL----ALRGVAFVIGNVSFFENNKDScgddgeqngddeevtrqqLEPMLGS---YWSSvATLRLSvelpeeedftLQDD 307
Cdd:cd01394  137 KLlsiaRKYDIPVVITNQVYSDIDDDR------------------LKPVGGTlleHWSK-AIIRLE----------KSPP 187

                        250       260
                 ....*....|....*....|....*...
gi 281362966 308 GLRFIYVISNTYGPDGEHCLLRITDAGV 335
Cdd:cd01394  188 GLRRATLEKHRSRPEGQSAGFRITDRGI 215
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 80-336 1.41e-10

archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a homolog of Rad51. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR)


Pssm-ID: 410923 [Multi-domain]  Cd Length: 233  Bit Score: 60.45  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDS-VEQPfkpgRVWELCGQPGVGKTQLLYTLALNFVWKHSQA-----VLFIDTKREFSCKRIQDMLRARE 153
Cdd:cd19515    3 TGSKELDKLLGGgIETQ----AITEVFGEFGSGKTQLCHQLAVNVQLPPEEGglngkAVYIDTENTFRPERIMQMAKALG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 154 VDeeaSERAMKGIRVVQAatgadINDllksfDHQ-LTAETHASM-----QTKLVLIDSLAACF-AFYRGRRMRDVRKSVL 226
Cdd:cd19515   79 LD---PDEVLDNIYVARA-----YNS-----NHQmLLVEKAEDLikegnNIKLLIVDSLTSHFrAEYVGRGTLAERQQKL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 227 TELACKIRKLA-LRGVAFVIGN-VSffeNNKDSCGDDGEQngddeevtrqqlePMLGSYWSSVATLRLSVELPEeedftl 304
Cdd:cd19515  146 NKHLHDLHRLAdLYNIAVLVTNqVM---AKPDAFFGDPTQ-------------AIGGHILGHAATFRVYLRKGK------ 203

                        250       260       270
                 ....*....|....*....|....*....|..
gi 281362966 305 qdDGLRFIYVISNTYGPDGEhCLLRITDAGVV 336
Cdd:cd19515  204 --GGKRIARLVDSPHLPEGE-AVFRITEKGIE 232
radA PRK04301
DNA repair and recombination protein RadA; Validated
 80-216 2.44e-10

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 60.66  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDS-VEQpfkpGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVL-----FIDTKREFSCKRIQDMLRARE 153
Cdd:PRK04301  86 TGSKELDELLGGgIET----QSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLegkavYIDTEGTFRPERIEQMAEALG 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 154 VDeeaSERAMKGIRVVQAatgadINDllksfDHQ-LTAETHASM-----QTKLVLIDSLAACF-AFYRGR 216
Cdd:PRK04301 162 LD---PDEVLDNIHVARA-----YNS-----DHQmLLAEKAEELikegeNIKLVIVDSLTAHFrAEYVGR 218
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 80-247 9.29e-10

Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.


Pssm-ID: 462471 [Multi-domain]  Cd Length: 255  Bit Score: 58.47  E-value: 9.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966   80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQ-----AVLFIDTKREFSCKRIQDMLRAREV 154
Cdd:pfam08423  21 TGSKELDKLLGG---GIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMgggegKALYIDTEGTFRPERLVAIAERYGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  155 DEEAserAMKGIRVVQAATGADINDLLksfdhQLTAETHASMQTKLVLIDSLAACF-AFYRGRRMRDVRKSVLTELACKI 233
Cdd:pfam08423  98 DPED---VLDNVAYARAYNSEHQMQLL-----QQAAAMMSESRFALLIVDSATALYrTDFSGRGELAERQQHLAKFLRTL 169

                         170
                  ....*....|....*
gi 281362966  234 RKLALR-GVAFVIGN 247
Cdd:pfam08423 170 QRLADEfGVAVVITN 184
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 99-292 8.19e-09

XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.


Pssm-ID: 410898 [Multi-domain]  Cd Length: 226  Bit Score: 55.05  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  99 GRVWELCGQPGVGKTQLLYTLALNFV----WK------HSQAVLFIDTKREFSCKRIQDMLRAR----------EVDEEA 158
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCIlpssWGgvplggLEAAVVFIDTDGRFDILRLRSILEARiraaiqaansSDDEED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 159 SERAMKGI-RVVQAATGADINDLLKSFD--HQLTAETHASMQTKLVLIDSLAA-----CFAFYRGRRMRDVRKSVLTELA 230
Cdd:cd19490   81 VEEIAREClQRLHIFRCHSSLQLLATLLslENYLLSLSANPELGLLLIDSISAfywqdRFSAELARAAPLLQEAALRAIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362966 231 CKIRKLALRGVAFVIG-NVSFFENNKDSCGDDGEQNGDDEEVTRQQLEPMlGSYWSSVATLRL 292
Cdd:cd19490  161 RELRRLRRRFQLVVIAtKQALFPGKSASTDNPAANNAVSKASAPSHREYL-PRPWQRLVTHRL 222
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
 80-247 1.91e-08

recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .


Pssm-ID: 410868 [Multi-domain]  Cd Length: 234  Bit Score: 54.07  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDS-VEQpfkpGRVWELCGQPGVGKTQLLYTLALNFVWKHSQA-----VLFIDTKREFSCKRIQDMLRARE 153
Cdd:cd01123    3 TGSKELDKLLGGgIET----GSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGggegkAIYIDTEGTFRPERLRAIAQRFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 154 VDEEAserAMKGIRVVQAATGadindllksfDHQL-----TAETHASMQTKLVLIDSLAACF-AFYRGRRMRDVRKSVLT 227
Cdd:cd01123   79 LDPDD---VLDNVAYARAFNS----------DHQTqlldqAAAMMVESRFKLLIVDSATALYrTDYSGRGELSARQMHLA 145

                        170       180
                 ....*....|....*....|.
gi 281362966 228 ELACKIRKLA-LRGVAFVIGN 247
Cdd:cd01123  146 KFLRMLQRLAdEFGVAVVVTN 166
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
 80-247 1.06e-06

homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.


Pssm-ID: 410922 [Multi-domain]  Cd Length: 236  Bit Score: 48.89  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLDSveqPFKPGRVWELCGQPGVGKTQLLYTLA----LNFVWKHSQA-VLFIDTKREFSCKRIQDMLRAREV 154
Cdd:cd19514    3 TGSTELDKLLGG---GIESMSITEVFGEFRTGKTQLSHTLCvtaqLPGSMGGGGGkVAYIDTEGTFRPDRIRPIAERFGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 155 DEEAserAMKGIRVVQAATGADINDLLKsfdhQLTAETHASMQTKLVLIDSLAACFAF-YRGRRMRDVRKSVLTELACKI 233
Cdd:cd19514   80 DHDA---VLDNILYARAYTSEHQMELLD----YVAAKFHEEAVFRLLIIDSIMALFRVdFSGRGELAERQQKLAQMLSRL 152

                        170
                 ....*....|....*
gi 281362966 234 RKLALR-GVAFVIGN 247
Cdd:cd19514  153 QKISEEyNVAVFITN 167
PTZ00035 PTZ00035
Rad51 protein; Provisional
 21-247 1.30e-05

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 46.14  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  21 LNLLRKNNICSLIDFYDADEKKLHELWAINIQSVRELKKELS-LLPKG------SVDEGTPDFNYDTGIEELDKLLDSve 93
Cdd:PTZ00035  36 IKKLKEAGICTVESVAYATKKDLCNIKGISEAKVEKIKEAASkLVPMGfisateYLEARKNIIRITTGSTQLDKLLGG-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  94 qPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQA-----VLFIDTKREFSCKRIQDMLRAREVDEEAserAMKGIRV 168
Cdd:PTZ00035 114 -GIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGggegkVLYIDTEGTFRPERIVQIAERFGLDPED---VLDNIAY 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 169 VQAATGADINDLLKSFDHQLTAETHAsmqtkLVLIDSLAACFAF-YRGRRMRDVRKSVLTELACKIRKLALR-GVAFVIG 246
Cdd:PTZ00035 190 ARAYNHEHQMQLLSQAAAKMAEERFA-----LLIVDSATALFRVdYSGRGELAERQQHLGKFLRALQKLADEfNVAVVIT 264


                 .
gi 281362966 247 N 247
Cdd:PTZ00035 265 N 265
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
80-241 1.66e-05

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 45.29  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLdsvEQPFKPGRVWELCGQPGVGKTqllyTLALNFVW---KHSQAVLFIDTkrEFSCKRIQDMLRAREVDE 156
Cdd:COG0467    4 TGIPGLDELL---GGGLPRGSSTLLSGPPGTGKT----TLALQFLAeglRRGEKGLYVSF--EESPEQLLRRAESLGLDL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 157 EASERAMKgIRVVQAATGADINDlLKSFDHQLtAETHASMQTKLVLIDSLAACFAFYRGRRMrdvRKSVLTELackIRKL 236
Cdd:COG0467   75 EEYIESGL-LRIIDLSPEELGLD-LEELLARL-REAVEEFGAKRVVIDSLSGLLLALPDPER---LREFLHRL---LRYL 145


                 ....*
gi 281362966 237 ALRGV 241
Cdd:COG0467  146 KKRGV 150
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 80-230 7.60e-05

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 43.41  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  80 TGIEELDKLLdsvEQPFKPGRVWELCGQPGVGKTqllyTLALNFVW---KHSQAVLFIDTKREfsckriQDMLRAR---- 152
Cdd:cd01124    3 TGIPGLDELL---GGGIPKGSVTLLTGGPGTGKT----LFGLQFLYagaKNGEPGLFFTFEES------PERLLRNaksf 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966 153 EVDEEASERAMKgIRVVQAAT----GADINDLLKSFDHQLtaethASMQTKLVLIDSLAACFAFYRGRRM--RDVRkSVL 226
Cdd:cd01124   70 GWDFDEMEDEGK-LIIVDAPPteagRFSLDELLSRILSII-----KSFKAKRVVIDSLSGLRRAKEDQMRarRIVI-ALL 142


                 ....
gi 281362966 227 TELA 230
Cdd:cd01124  143 NELR 146
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
 80-237 7.23e-04

meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.


Pssm-ID: 131292 [Multi-domain]  Cd Length: 313  Bit Score: 40.92  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966   80 TGIEELDKLLDSVEQPFKpgrVWELCGQPGVGKTQLLYTLALNFVWKHSQA-----VLFIDTKREFSCKRIQDMLRAREV 154
Cdd:TIGR02238  80 TGSQALDGILGGGIESMS---ITEVFGEFRCGKTQLSHTLCVTAQLPREMGggngkVAYIDTEGTFRPDRIRAIAERFGV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362966  155 DEEAserAMKGIRVVQAATGADINDLLKsfdhQLTAETHaSMQTKLVLIDSLAACFAF-YRGRRMRDVRKSVLTELACKI 233
Cdd:TIGR02238 157 DPDA---VLDNILYARAYTSEHQMELLD----YLAAKFS-EEPFRLLIVDSIMALFRVdFSGRGELSERQQKLAQMLSRL 228


                  ....
gi 281362966  234 RKLA 237
Cdd:TIGR02238 229 NKIS 232
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 75-120 1.65e-03

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 40.48  E-value: 1.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 281362966    75 DFNYDTGIE-ELDKLLDSVEQPFKPGRVWELCGQPGVGKTQLLYTLA 120
Cdd:TIGR00956  764 NLTYEVKIKkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA 810
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 98-172 7.56e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 7.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362966    98 PGRVWELCGQPGVGKTQLLYTLALNFVwKHSQAVLFIDTKREFSCKRIQDMLRAREVDEEASERAMKGIRVVQAA 172
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 80-134 7.80e-03

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 37.49  E-value: 7.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 281362966  80 TGIEELDKLLdsveQPFKPGRVWELCGQPGVGKTQLLYTLALNFVWKHSQAVLFI 134
Cdd:cd00984    4 TGFTDLDKLT----GGLQPGDLIIIAARPSMGKTAFALNIAENIALDEGLPVLFF 54
 
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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