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Conserved domains on  [gi|195399463|ref|XP_002058339|]
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DNA repair protein RAD51 homolog 3 isoform X1 [Drosophila virilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 35-244 2.62e-72

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: 218.25  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  35 GKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFnparlkeladdlaarlrctsisaptatqmlqNV 114
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF-------------------------------NI 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 115 YYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRMVNNVS-DRTELLMEVHDGMRKLQLMHDLAFVITNNQGY 193
Cdd:cd19492   50 HYFRVHDYVELLALINSLPKFLEDHPKVKLIVVDSIAFPFRHDFDDLaQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTT 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195399463 194 RRRMS-QFQLEAVLGRKHSQLINKRIWLTENEcfvgkraktKRLICKLLKYT 244
Cdd:cd19492  130 KISEDgQSQLVPALGESWSHACTTRLFLTWDE---------KQRFAHLYKSP 172
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 17-51 1.90e-06

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 cd19488:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 225  Bit Score: 47.34  E-value: 1.90e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQL 51
Cdd:cd19488    1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTL 35
 
Name Accession Description Interval E-value
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 35-244 2.62e-72

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: 218.25  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  35 GKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFnparlkeladdlaarlrctsisaptatqmlqNV 114
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF-------------------------------NI 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 115 YYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRMVNNVS-DRTELLMEVHDGMRKLQLMHDLAFVITNNQGY 193
Cdd:cd19492   50 HYFRVHDYVELLALINSLPKFLEDHPKVKLIVVDSIAFPFRHDFDDLaQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTT 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195399463 194 RRRMS-QFQLEAVLGRKHSQLINKRIWLTENEcfvgkraktKRLICKLLKYT 244
Cdd:cd19492  130 KISEDgQSQLVPALGESWSHACTTRLFLTWDE---------KQRFAHLYKSP 172
radA PRK04301
DNA repair and recombination protein RadA; Validated
 2-189 1.16e-28

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 110.35  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   2 EYKTAKNLKAEKSPT--ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRK 79
Cdd:PRK04301  67 GFETALEVLERRKNVgkITTGSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAVYIDTEG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  80 DFNPARLKELADDLAARLRctsisaptatQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRM--- 156
Cdd:PRK04301 147 TFRPERIEQMAEALGLDPD----------EVLDNIHVARAYNSDHQMLLAEKAEELIKEGENIKLVIVDSLTAHFRAeyv 216

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 195399463 157 -VNNVSDRTELLME-VHDGMRkLQLMHDLAFVITN 189
Cdd:PRK04301 217 gRGNLAERQQKLNKhLHDLLR-LADLYNAAVVVTN 250
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 17-189 2.33e-23

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: 94.68  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:pfam08423  19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTEGTFRPERLVAIAERYGL- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   97 lrctsisapTATQMLQNVYYVDCRNTA------QLVAGLLNCHKYlekepniKLIIVDSISFAIRmvNNVSDRTELL--- 167
Cdd:pfam08423  98 ---------DPEDVLDNVAYARAYNSEhqmqllQQAAAMMSESRF-------ALLIVDSATALYR--TDFSGRGELAerq 159

                         170       180
                  ....*....|....*....|....*
gi 195399463  168 MEVHDGMRKLQLM---HDLAFVITN 189
Cdd:pfam08423 160 QHLAKFLRTLQRLadeFGVAVVITN 184
recomb_radA TIGR02236
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ...
 3-189 4.51e-23

DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 131290 [Multi-domain]  Cd Length: 310  Bit Score: 95.20  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463    3 YKTAKNLKAEKSPT--ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKD 80
Cdd:TIGR02236  61 FETADDVLERRKTIgkITTGSKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   81 FNPARLKELADDLAARLRctsisaptatQMLQNVYYVDCRNTAQLVAgLLNCHKYLEKE--PNIKLIIVDSISFAIRMV- 157
Cdd:TIGR02236 141 FRPERIMQMAEARGLDPD----------EVLKNIYVARAYNSNHQML-LVEKAEDLIKElnNPVKLLIVDSLTSHFRAEy 209

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 195399463  158 ---NNVSDRTELL-MEVHDGMRkLQLMHDLAFVITN 189
Cdd:TIGR02236 210 vgrGALAERQQKLnKHLHDLLR-LADLYNAAVVVTN 244
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
17-177 1.75e-11

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 61.86  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNvqipryACGLASKALYFDTRKDfnPARLKELADDLAAR 96
Cdd:COG0467    2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAE------GLRRGEKGLYVSFEES--PEQLLRRAESLGLD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 LRctsisaptatQMLQN--VYYVDCR------NTAQLVAGLlncHKYLEKEpNIKLIIVDSISFAIRMVNNVSDRTELLM 168
Cdd:COG0467   74 LE----------EYIESglLRIIDLSpeelglDLEELLARL---REAVEEF-GAKRVVIDSLSGLLLALPDPERLREFLH 139


                 ....*....
gi 195399463 169 EVHDGMRKL 177
Cdd:COG0467  140 RLLRYLKKR 148
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 17-51 1.90e-06

N-terminal domain of KaiC family protein; uncharacterized subfamily; 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: 410896 [Multi-domain]  Cd Length: 225  Bit Score: 47.34  E-value: 1.90e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQL 51
Cdd:cd19488    1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTL 35
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 34-190 2.44e-04

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: 40.43  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463    34 PGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACglaskaLYFDTRKDFNPARLKELADDLAARLRcTSISAPTATQMLQN 113
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------IYIDGEDILEEVLDQLLLIIVGGKKA-SGSGELRLRLALAL 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195399463   114 VyyvdcrntaqlvagllnchkyleKEPNIKLIIVDSISfaiRMVNNVSDRTELLMEVHDGMRKLQLMHDLAFVITNN 190
Cdd:smart00382  74 A-----------------------RKLKPDVLILDEIT---SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
PRK04328 PRK04328
hypothetical protein; Provisional
 15-52 5.60e-03

hypothetical protein; Provisional


Pssm-ID: 235281  Cd Length: 249  Bit Score: 36.98  E-value: 5.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 195399463  15 PTITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLC 52
Cdd:PRK04328   3 KRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFS 40
 
Name Accession Description Interval E-value
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 35-244 2.62e-72

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: 218.25  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  35 GKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFnparlkeladdlaarlrctsisaptatqmlqNV 114
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF-------------------------------NI 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 115 YYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRMVNNVS-DRTELLMEVHDGMRKLQLMHDLAFVITNNQGY 193
Cdd:cd19492   50 HYFRVHDYVELLALINSLPKFLEDHPKVKLIVVDSIAFPFRHDFDDLaQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTT 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195399463 194 RRRMS-QFQLEAVLGRKHSQLINKRIWLTENEcfvgkraktKRLICKLLKYT 244
Cdd:cd19492  130 KISEDgQSQLVPALGESWSHACTTRLFLTWDE---------KQRFAHLYKSP 172
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
 24-189 1.41e-34

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: 124.33  E-value: 1.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  24 LDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAARlrctsIS 103
Cdd:cd19491    1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSLPKR-----YH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 104 APTATQMLQNVYYVDCRNTAQlvagLLNCHKY----LEKEPNIKLIIVDSISFAIR-----MVNNVSDRTELLMEVHDGM 174
Cdd:cd19491   76 LEKAKNFLDNIFVEHVADLET----LEHCLNYqlpaLLERGPIRLVVIDSIAALFRsefdtSRSDLVERAKYLRRLADHL 151

                        170
                 ....*....|....*
gi 195399463 175 RKLQLMHDLAFVITN 189
Cdd:cd19491  152 KRLADKYNLAVVVVN 166
radA PRK04301
DNA repair and recombination protein RadA; Validated
 2-189 1.16e-28

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 110.35  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   2 EYKTAKNLKAEKSPT--ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRK 79
Cdd:PRK04301  67 GFETALEVLERRKNVgkITTGSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAVYIDTEG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  80 DFNPARLKELADDLAARLRctsisaptatQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRM--- 156
Cdd:PRK04301 147 TFRPERIEQMAEALGLDPD----------EVLDNIHVARAYNSDHQMLLAEKAEELIKEGENIKLVIVDSLTAHFRAeyv 216

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 195399463 157 -VNNVSDRTELLME-VHDGMRkLQLMHDLAFVITN 189
Cdd:PRK04301 217 gRGNLAERQQKLNKhLHDLLR-LADLYNAAVVVTN 250
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 29-225 4.50e-26

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: 100.79  E-value: 4.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  29 RGGIRPGKVYELVGKPGTGKTQLCMKLCLNVqipryACGLASKALYFDTRKDFNPARLKELADDLAArlrctsiSAPTAT 108
Cdd:cd19489    1 GGGLRTGEITELVGESSSGKTQLCLTAAANV-----ASRSGQNVLYIDTKSSFSARRLAQILKSRAQ-------DAEEID 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 109 QMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPN-----IKLIIVDSISFAIRMVNNVSDRTE---LLMEVHDGMRKLQLM 180
Cdd:cd19489   69 KALQRIRVVRVFDPYELLDLLEELRNTLSQQQEnlysrLKLVIIDSLSALISPLLGGSKHSEghaLLASLARLLKKLAAE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 195399463 181 HDLAFVITNNQ-GYRRRMSQFQLEAVLGRKHSQLINKRIWLTENEC 225
Cdd:cd19489  149 YQIAVLVTNLTvRGGDGGQQGSTKPALGEYWESVPSTRLLLSRDEN 194
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 17-189 7.57e-26

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: 100.90  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:cd19515    1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERIMQMAKALGL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 lrctsisapTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRMV----NNVSDRTELLME-VH 171
Cdd:cd19515   80 ---------DPDEVLDNIYVARAYNSNHQMLLVEKAEDLIKEGNNIKLLIVDSLTSHFRAEyvgrGTLAERQQKLNKhLH 150

                        170
                 ....*....|....*...
gi 195399463 172 DGMRkLQLMHDLAFVITN 189
Cdd:cd19515  151 DLHR-LADLYNIAVLVTN 167
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
 1-189 8.66e-25

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 100.19  E-value: 8.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   1 MEYKTAKNLKAEKSPTI--TTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTR 78
Cdd:PLN03186  87 LGFTTASQLHAQRQEIIqiTTGSRELDKILEGGIETGSITEIYGEFRTGKTQLCHTLCVTCQLPLDQGGGEGKAMYIDTE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  79 KDFNPARLKELADdlaaRLRCTSisaptaTQMLQNVYYVDCRNTAQLvAGLLNCHKYLEKEPNIKLIIVDSISFAIRmvN 158
Cdd:PLN03186 167 GTFRPQRLIQIAE----RFGLNG------ADVLENVAYARAYNTDHQ-SELLLEAASMMAETRFALMIVDSATALYR--T 233

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 195399463 159 NVSDRTEL-LMEVHDG--MRKLQLMHD---LAFVITN 189
Cdd:PLN03186 234 EFSGRGELsARQMHLGkfLRSLQRLADefgVAVVITN 270
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
 17-189 5.63e-24

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: 96.06  E-value: 5.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:cd01123    1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERLRAIAQRFGL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 lrctsisapTATQMLQNVYYVDCRNTAQLVAgLLNCHKYLEKEPNIKLIIVDSISFAIRmvNNVSDRTELL---MEVHDG 173
Cdd:cd01123   80 ---------DPDDVLDNVAYARAFNSDHQTQ-LLDQAAAMMVESRFKLLIVDSATALYR--TDYSGRGELSarqMHLAKF 147

                        170
                 ....*....|....*....
gi 195399463 174 MRKLQLMHDL---AFVITN 189
Cdd:cd01123  148 LRMLQRLADEfgvAVVVTN 166
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
 17-189 1.56e-23

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: 94.73  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:cd19514    1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRIRPIAERFGV- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 lrctsisapTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPNIKLIIVDSISFAIRM----VNNVSDRTELLMEVHD 172
Cdd:cd19514   80 ---------DHDAVLDNILYARAYTSEHQMELLDYVAAKFHEEAVFRLLIIDSIMALFRVdfsgRGELAERQQKLAQMLS 150

                        170
                 ....*....|....*..
gi 195399463 173 GMRKLQLMHDLAFVITN 189
Cdd:cd19514  151 RLQKISEEYNVAVFITN 167
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 17-189 2.33e-23

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: 94.68  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:pfam08423  19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTEGTFRPERLVAIAERYGL- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   97 lrctsisapTATQMLQNVYYVDCRNTA------QLVAGLLNCHKYlekepniKLIIVDSISFAIRmvNNVSDRTELL--- 167
Cdd:pfam08423  98 ---------DPEDVLDNVAYARAYNSEhqmqllQQAAAMMSESRF-------ALLIVDSATALYR--TDFSGRGELAerq 159

                         170       180
                  ....*....|....*....|....*
gi 195399463  168 MEVHDGMRKLQLM---HDLAFVITN 189
Cdd:pfam08423 160 QHLAKFLRTLQRLadeFGVAVVITN 184
recomb_radA TIGR02236
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ...
 3-189 4.51e-23

DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 131290 [Multi-domain]  Cd Length: 310  Bit Score: 95.20  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463    3 YKTAKNLKAEKSPT--ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKD 80
Cdd:TIGR02236  61 FETADDVLERRKTIgkITTGSKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   81 FNPARLKELADDLAARLRctsisaptatQMLQNVYYVDCRNTAQLVAgLLNCHKYLEKE--PNIKLIIVDSISFAIRMV- 157
Cdd:TIGR02236 141 FRPERIMQMAEARGLDPD----------EVLKNIYVARAYNSNHQML-LVEKAEDLIKElnNPVKLLIVDSLTSHFRAEy 209

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 195399463  158 ---NNVSDRTELL-MEVHDGMRkLQLMHDLAFVITN 189
Cdd:TIGR02236 210 vgrGALAERQQKLnKHLHDLLR-LADLYNAAVVVTN 244
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 25-221 2.89e-22

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: 91.23  E-value: 2.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  25 DKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAARLRCTSISA 104
Cdd:cd19493    1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFSGFMEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 105 P-TATQMLQNVYYVDCRNTAQLVAGLLNCHKYLeKEPNIKLIIVDSISFAIR-----MVNNVSDRTELLMEVHDGMRKLQ 178
Cdd:cd19493   81 NeRAEEMLKRVAVVRVTTLAQLLERLPNLEEHI-LSSGVRLVVIDSIAALVRrefggSDGEVTERHNALAREASSLKRLA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 195399463 179 LMHDLAFVITNNQGYRRRMSQFQ---LEAVLGRKHSQLINKRIWLT 221
Cdd:cd19493  160 EEFRIAVLVTNQATTHFGDAGDGssgVTAALGDAWAHAVNTRLRLE 205
PTZ00035 PTZ00035
Rad51 protein; Provisional
 17-189 9.30e-22

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 91.98  E-value: 9.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELAD--DLa 94
Cdd:PTZ00035 100 ITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAErfGL- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  95 arlrctsisapTATQMLQNVYYVDCRNTAQLVAgLLNCHKYLEKEPNIKLIIVDSISFAIRMvnNVSDRTELL---MEVH 171
Cdd:PTZ00035 179 -----------DPEDVLDNIAYARAYNHEHQMQ-LLSQAAAKMAEERFALLIVDSATALFRV--DYSGRGELAerqQHLG 244

                        170       180
                 ....*....|....*....|.
gi 195399463 172 DGMRKLQLMHD---LAFVITN 189
Cdd:PTZ00035 245 KFLRALQKLADefnVAVVITN 265
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
 17-189 2.57e-21

RAD51D recombinase; RAD51 recombinase plays an essential 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. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.


Pssm-ID: 410921 [Multi-domain]  Cd Length: 235  Bit Score: 88.91  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:cd19513    1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAERYGL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 lrctsisapTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLeKEPNIKLIIVDSISFAIRmvNNVSDRTELL---MEVHDG 173
Cdd:cd19513   80 ---------NGEDVLDNVAYARAYNTDHQMQLLIQASAMM-AESRYALLIVDSATALYR--TDYSGRGELSarqMHLAKF 147

                        170
                 ....*....|....*....
gi 195399463 174 MRKLQLMHD---LAFVITN 189
Cdd:cd19513  148 LRMLQRLADefgVAVVITN 166
recomb_RAD51 TIGR02239
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ...
 1-189 3.83e-20

DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).


Pssm-ID: 274048 [Multi-domain]  Cd Length: 316  Bit Score: 87.09  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463    1 MEYKTAKNLKAEKSP--TITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTR 78
Cdd:TIGR02239  60 MGFTTATEFHQRRQEviQLTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   79 KDFNPARLKELADDLAArlrctsisapTATQMLQNVYYVDCRNTAQLVAgLLNCHKYLEKEPNIKLIIVDSISFAIRmvN 158
Cdd:TIGR02239 140 GTFRPERLLAIAERYGL----------NPEDVLDNVAYARAYNTDHQLQ-LLQQAAAMMSESRFALLIVDSATALYR--T 206

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 195399463  159 NVSDRTEL-LMEVHDG--MRKLQLMHD---LAFVITN 189
Cdd:TIGR02239 207 DFSGRGELsARQMHLArfLRSLQRLADefgVAVVITN 243
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
 17-189 6.32e-18

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: 80.98  E-value: 6.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKDFNPARLKELADDLAAr 96
Cdd:TIGR02238  78 ITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAERFGV- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   97 lrctsisapTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPnIKLIIVDSISFAIRM----VNNVSDRTELLMEVHD 172
Cdd:TIGR02238 157 ---------DPDAVLDNILYARAYTSEHQMELLDYLAAKFSEEP-FRLLIVDSIMALFRVdfsgRGELSERQQKLAQMLS 226

                         170
                  ....*....|....*..
gi 195399463  173 GMRKLQLMHDLAFVITN 189
Cdd:TIGR02238 227 RLNKISEEFNVAVFVTN 243
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 35-220 1.57e-17

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: 77.39  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  35 GKVYELVGKPGTGKTQLCMKLCLNVQIpryacgLASKALYFDTRKDFNPARLKELADdlaarlrctsiSAPTATQ----M 110
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALL------LGGGVVWIDTEGAFPPSRLVQILE-----------ASPSSELelaeA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 111 LQNVYYVDCRNT-AQLVAglLNCH-KYLEKEPNIKLIIVDSISFAIR--------MVNNVSDRTELLMEVHDGMRKLQLM 180
Cdd:cd01393   64 LSRLLYFRPPDTlAHLLA--LDSLpESLFPPPNTSLVVVDSVSALFRkafprggdGDSSSSLRARLLSQLARALQKLAAQ 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 195399463 181 HDLAFVITnNQGYRRRMSQFQLE---AVLGRKHSQLINKRIWL 220
Cdd:cd01393  142 FNLAVVVT-NQVTTKIRGGSGASlvpPALGNTWEHSVSTRLLL 183
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 35-151 2.47e-16

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: 75.08  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  35 GKVYELVGKPGTGKTQLCMKLCLNVQIPR-----YACGLASKALYFDTRKDFNPARLKELaddLAARLR------CTSIS 103
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCILPSswggvPLGGLEAAVVFIDTDGRFDILRLRSI---LEARIRaaiqaaNSSDD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 195399463 104 APTATQM----LQNVYYVDCRNTAQLVAGLLNCHKYLEK---EPNIKLIIVDSIS 151
Cdd:cd19490   78 EEDVEEIarecLQRLHIFRCHSSLQLLATLLSLENYLLSlsaNPELGLLLIDSIS 132
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 17-189 9.81e-16

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: 73.50  E-value: 9.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQipryACGLasKALYFDTrKDFNPARLKELADDLAAR 96
Cdd:cd01394    1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAA----KQGK--KVVYIDT-EGLSPERFQQIAGERFES 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 LrctsisaptatqmLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPnIKLIIVDSISFAIRMvnNVSDRTELLMEVHDGMRK 176
Cdd:cd01394   74 I-------------ASNIIVFEPYSFDEQGVAIQEAEKLLKSDK-VDLVVVDSATALYRL--ELGDDSEANRELSRQMSK 137

                        170
                 ....*....|....*.
gi 195399463 177 LQLM---HDLAFVITN 189
Cdd:cd01394  138 LLSIarkYDIPVVITN 153
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 17-189 1.22e-15

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 73.36  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNvqipryACGLASKALYFDTrKDFNPARLKELADDLAAR 96
Cdd:PRK09361   5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVE------AAKNGKKVIYIDT-EGLSPERFKQIAGEDFEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 LrctsisaptatqmLQNVY----------YVDCRNTAQLVagllnchkylekEPNIKLIIVDSISFAIRM-VNNVSDRTE 165
Cdd:PRK09361  78 L-------------LSNIIifepssfeeqSEAIRKAEKLA------------KENVGLIVLDSATSLYRLeLEDEEDNSK 132

                        170       180
                 ....*....|....*....|....*..
gi 195399463 166 LLMEVHDGMRKLQLM---HDLAFVITN 189
Cdd:PRK09361 133 LNRELGRQLTHLLKLarkHDLAVVITN 159
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
 3-189 9.77e-15

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 72.50  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463   3 YKTAKNLKAEKSPT--ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACGLASKALYFDTRKD 80
Cdd:PLN03187  92 FITGSDALLKRKSVvrITTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGGGNGKVAYIDTEGT 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  81 FNPARLKELADDLAArlrctsisapTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLEKEPnIKLIIVDSISFAIRM---- 156
Cdd:PLN03187 172 FRPDRIVPIAERFGM----------DADAVLDNIIYARAYTYEHQYNLLLGLAAKMAEEP-FRLLIVDSVIALFRVdftg 240

                        170       180       190
                 ....*....|....*....|....*....|...
gi 195399463 157 VNNVSDRTELLMEVHDGMRKLQLMHDLAFVITN 189
Cdd:PLN03187 241 RGELAERQQKLAQMLSRLTKIAEEFNVAVYMTN 273
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
17-177 1.75e-11

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 61.86  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNvqipryACGLASKALYFDTRKDfnPARLKELADDLAAR 96
Cdd:COG0467    2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAE------GLRRGEKGLYVSFEES--PEQLLRRAESLGLD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  97 LRctsisaptatQMLQN--VYYVDCR------NTAQLVAGLlncHKYLEKEpNIKLIIVDSISFAIRMVNNVSDRTELLM 168
Cdd:COG0467   74 LE----------EYIESglLRIIDLSpeelglDLEELLARL---REAVEEF-GAKRVVIDSLSGLLLALPDPERLREFLH 139


                 ....*....
gi 195399463 169 EVHDGMRKL 177
Cdd:COG0467  140 RLLRYLKKR 148
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
32-187 1.53e-07

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 51.05  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  32 IRPGKVYELVGKPGTGKTQLCMKLCLNVqipryACGL--------ASKALYF---DTRKDFNPaRLKELADDLaarlrct 100
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQLAAAV-----AAGGpwlgrrvpPGKVLYLaaeDDRGELRR-RLKALGADL------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463 101 sisAPTATQMLQNVYYVDCRNTAQLVAGLLNCHKYLEkEPNIKLIIVDSISFAIRMVNNVSDRTELLMEVhdgMRKLQLM 180
Cdd:COG3598   77 ---GLPFADLDGRLRLLSLAGDLDDTDDLEALERAIE-EEGPDLVVIDPLARVFGGDENDAEEMRAFLNP---LDRLAER 149


                 ....*..
gi 195399463 181 HDLAFVI 187
Cdd:COG3598  150 TGAAVLL 156
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 17-53 4.42e-07

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: 49.18  E-value: 4.42e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCM 53
Cdd:cd01124    1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGL 37
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 17-51 1.90e-06

N-terminal domain of KaiC family protein; uncharacterized subfamily; 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: 410896 [Multi-domain]  Cd Length: 225  Bit Score: 47.34  E-value: 1.90e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQL 51
Cdd:cd19488    1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTL 35
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 19-54 8.32e-05

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 42.62  E-value: 8.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 195399463   19 TGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMK 54
Cdd:pfam06745   3 TGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQ 38
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 34-190 2.44e-04

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: 40.43  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463    34 PGKVYELVGKPGTGKTQLCMKLCLNVQIPRYACglaskaLYFDTRKDFNPARLKELADDLAARLRcTSISAPTATQMLQN 113
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------IYIDGEDILEEVLDQLLLIIVGGKKA-SGSGELRLRLALAL 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195399463   114 VyyvdcrntaqlvagllnchkyleKEPNIKLIIVDSISfaiRMVNNVSDRTELLMEVHDGMRKLQLMHDLAFVITNN 190
Cdd:smart00382  74 A-----------------------RKLKPDVLILDEIT---SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 10-74 3.46e-04

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 40.98  E-value: 3.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195399463  10 KAEKSPTITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVqipryaCGLASKALY 74
Cdd:cd01121   57 EAEEEERISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARL------AQRGGKVLY 115
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
10-60 6.92e-04

RecA/RadA recombinase [Replication, recombination and repair];


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 40.15  E-value: 6.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195399463  10 KAEKSPTITTGITALDKCL-RGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQ 60
Cdd:COG0468   37 ARQDVEVISTGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 88
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 17-59 1.08e-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: 39.42  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 195399463  17 ITTGITALDKcLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNV 59
Cdd:cd00984    2 LPTGFTDLDK-LTGGLQPGDLIIIAARPSMGKTAFALNIAENI 43
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 15-60 2.31e-03

recombinase A; 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.


Pssm-ID: 410863 [Multi-domain]  Cd Length: 235  Bit Score: 38.31  E-value: 2.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 195399463  15 PTITTGITALDKCLR-GGIRPGKVYELVGKPGTGKTQLCMKLCLNVQ 60
Cdd:cd00983    3 EVIPTGSLSLDIALGiGGLPRGRIIEIYGPESSGKTTLALHAIAEAQ 49
PRK07773 PRK07773
replicative DNA helicase; Validated
 10-148 4.86e-03

replicative DNA helicase; Validated


Pssm-ID: 236093 [Multi-domain]  Cd Length: 886  Bit Score: 37.81  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195399463  10 KAEKSPTITTGITALDKcLRGGIRPGKVYELVGKPGTGKTQLCMKLCLNVQIPRY-----------ACGLASKALYFDTR 78
Cdd:PRK07773 193 SGGLARGVPTGFTELDA-MTNGLHPGQLIIVAARPSMGKTTFGLDFARNCAIRHRlavaifslemsKEQLVMRLLSAEAK 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195399463  79 KDFNPARLKELADD----LAARLRCTSiSAPTATQMLQNVYYVDCRNTAqlvagllnchKYLEKEPNIKLIIVD 148
Cdd:PRK07773 272 IKLSDMRSGRMSDDdwtrLARAMGEIS-EAPIFIDDTPNLTVMEIRAKA----------RRLRQEANLGLIVVD 334
PRK04328 PRK04328
hypothetical protein; Provisional
 15-52 5.60e-03

hypothetical protein; Provisional


Pssm-ID: 235281  Cd Length: 249  Bit Score: 36.98  E-value: 5.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 195399463  15 PTITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLC 52
Cdd:PRK04328   3 KRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFS 40
KaiC_arch cd19486
KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; KaiC ...
 17-58 5.68e-03

KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; 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: 410894  Cd Length: 230  Bit Score: 37.07  E-value: 5.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 195399463  17 ITTGITALDKCLRGGIRPGKVYELVGKPGTGKTQLCMKLCLN 58
Cdd:cd19486    1 VKTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWN 42
 
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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