|
Name |
Accession |
Description |
Interval |
E-value |
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-361 |
3.96e-149 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 425.23 E-value: 3.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQN--Q 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGdrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 79 VFHTLSIQVDKRGKKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALD 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 159 QRNAAIKTQ-----DYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWDNTLKETLSLRYESSlittesPTLNDIA 233
Cdd:TIGR00611 161 QRNAALKQAqrqygDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYR------GELWDKE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 234 SNYYEQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHAC 313
Cdd:TIGR00611 235 TDYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 497916067 314 LDQNRLDQLFQLSTSLGQTVTTSTICPNHLDSNSSIFHVTQAQVSLVT 361
Cdd:TIGR00611 315 LDDQRRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVTIALVSVDR 362
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-358 |
7.98e-130 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 376.04 E-value: 7.98e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVF 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 81 HTLSIQVDKRG-KKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQ 159
Cdd:PRK00064 81 LPLGLEIDKKGgRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 160 RNAAIKTQDYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWD--NTLKETLSLRYESSLitteSPTLNDIASNYY 237
Cdd:PRK00064 161 RNALLKQADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQeiSPEFELASLSYQSSV----EDDAEKIEEDLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 238 EQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLDQN 317
Cdd:PRK00064 237 EALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 497916067 318 RLDQLFQLSTSLGQTVTTSTICPNHLDS---NSSIFHVTQAQVS 358
Cdd:PRK00064 317 RRAALLERLKGLGAQVFITTTDLEDLADlleNAKIFHVEQGKIT 360
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-337 |
1.73e-110 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 326.34 E-value: 1.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 2 RVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVFH 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 82 TLSIQVDKRGKKILF-DGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQR 160
Cdd:COG1195 81 RLGLGLSRGGKKRVRiNGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 161 NAAIKTQ---DYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWDN--TLKETLSLRYESSLITTESptlnDIASN 235
Cdd:COG1195 161 NALLKQGreaDLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAAlsGGKEELELRYRSGWLYESA----ELEEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 236 YYEQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLD 315
Cdd:COG1195 237 LLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELD 316
|
330 340
....*....|....*....|...
gi 497916067 316 QNRLDQLFQ-LSTSLGQTVTTST 337
Cdd:COG1195 317 EERREALLElLADLGGQVFITTT 339
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
5-358 |
8.29e-59 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 191.36 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 5 SLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVFHTLS 84
Cdd:cd03242 3 SLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 85 IQVDK-RGKKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQRNAA 163
Cdd:cd03242 83 LTIRSgGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRNAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 164 IKtqdyktiaawnspliaygslvallryecakklhkifqnlwdntlketlslryesslittesptlndiasnyyeqlrla 243
Cdd:cd03242 163 LK------------------------------------------------------------------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 244 ntkdfelgyttvGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLDQNRLDQLF 323
Cdd:cd03242 165 ------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALL 232
|
330 340 350
....*....|....*....|....*....|....*...
gi 497916067 324 QLSTSLGQT-VTTSTIC--PNHLDSNSSIFHVTQAQVS 358
Cdd:cd03242 233 DAIEGRVQTfVTTTDLAdfDALWLRRAQIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-172 |
2.64e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 3 VHSLFLKDFRNYSE-LRLELGPEMNSIFGLNAQGKTNILEA-LYILSL--GRSFRTSRLTEAIRFGSSHF----FIEAVF 74
Cdd:pfam02463 2 LKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAiLFVLGErsAKSLRSERLSDLIHSKSGAFvnsaEVEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 75 --SQNQVFH-----TLSIQVDKRGK-KILFDGAPITKlSALVGLFPVILFSVKDTTIIEGSPAERRrfldllLAQASEKY 146
Cdd:pfam02463 82 dnEDHELPIdkeevSIRRRVYRGGDsEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEI------IAMMKPER 154
|
170 180 190
....*....|....*....|....*....|...
gi 497916067 147 TGQI------ALYHKALDQRNAA-IKTQDYKTI 172
Cdd:pfam02463 155 RLEIeeeaagSRLKRKKKEALKKlIEETENLAE 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-361 |
3.96e-149 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 425.23 E-value: 3.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQN--Q 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGdrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 79 VFHTLSIQVDKRGKKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALD 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 159 QRNAAIKTQ-----DYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWDNTLKETLSLRYESSlittesPTLNDIA 233
Cdd:TIGR00611 161 QRNAALKQAqrqygDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYR------GELWDKE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 234 SNYYEQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHAC 313
Cdd:TIGR00611 235 TDYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 497916067 314 LDQNRLDQLFQLSTSLGQTVTTSTICPNHLDSNSSIFHVTQAQVSLVT 361
Cdd:TIGR00611 315 LDDQRRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVTIALVSVDR 362
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-358 |
7.98e-130 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 376.04 E-value: 7.98e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVF 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 81 HTLSIQVDKRG-KKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQ 159
Cdd:PRK00064 81 LPLGLEIDKKGgRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 160 RNAAIKTQDYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWD--NTLKETLSLRYESSLitteSPTLNDIASNYY 237
Cdd:PRK00064 161 RNALLKQADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQeiSPEFELASLSYQSSV----EDDAEKIEEDLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 238 EQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLDQN 317
Cdd:PRK00064 237 EALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 497916067 318 RLDQLFQLSTSLGQTVTTSTICPNHLDS---NSSIFHVTQAQVS 358
Cdd:PRK00064 317 RRAALLERLKGLGAQVFITTTDLEDLADlleNAKIFHVEQGKIT 360
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-337 |
1.73e-110 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 326.34 E-value: 1.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 2 RVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVFH 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 82 TLSIQVDKRGKKILF-DGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQR 160
Cdd:COG1195 81 RLGLGLSRGGKKRVRiNGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 161 NAAIKTQ---DYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWDN--TLKETLSLRYESSLITTESptlnDIASN 235
Cdd:COG1195 161 NALLKQGreaDLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAAlsGGKEELELRYRSGWLYESA----ELEEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 236 YYEQLRLANTKDFELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLD 315
Cdd:COG1195 237 LLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELD 316
|
330 340
....*....|....*....|...
gi 497916067 316 QNRLDQLFQ-LSTSLGQTVTTST 337
Cdd:COG1195 317 EERREALLElLADLGGQVFITTT 339
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-342 |
9.46e-63 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 204.25 E-value: 9.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYiLSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVF 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIY-LALTGELPNGRLADLVRFGEGEAWVHAEVETGGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 81 HTLSIQVDKRGKKILFDGAPItKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQR 160
Cdd:PRK14079 80 SRLEVGLGPGRRELKLDGVRV-SLRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYERAVQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 161 NAAIKTQDYKTIAAWNSPLIAYGSLVALLRYECAKKLHKIFQNLWDNTLKETlSLRYESSLITTESPTLNDIASNYYEQL 240
Cdd:PRK14079 159 NAALKSGGGWGLHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRK-PLRLELSESTAPEGYLAALEARRAEEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 241 rlantkdfELGYTTVGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLDQNRLD 320
Cdd:PRK14079 238 --------ARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELDPRRRG 309
|
330 340
....*....|....*....|..
gi 497916067 321 QLFQLSTSLGQTVTTSTICPNH 342
Cdd:PRK14079 310 ALLALAASLPQAIVAGTEAPPG 331
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
5-358 |
8.29e-59 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 191.36 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 5 SLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQNQVFHTLS 84
Cdd:cd03242 3 SLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 85 IQVDK-RGKKILFDGAPITKLSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYTGQIALYHKALDQRNAA 163
Cdd:cd03242 83 LTIRSgGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRNAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 164 IKtqdyktiaawnspliaygslvallryecakklhkifqnlwdntlketlslryesslittesptlndiasnyyeqlrla 243
Cdd:cd03242 163 LK------------------------------------------------------------------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 244 ntkdfelgyttvGPHRDELIITLNDLPVSKFSSEGQKHSLLAVLRFAECVYLQEEFLIHPLLCMDDIHACLDQNRLDQLF 323
Cdd:cd03242 165 ------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALL 232
|
330 340 350
....*....|....*....|....*....|....*...
gi 497916067 324 QLSTSLGQT-VTTSTIC--PNHLDSNSSIFHVTQAQVS 358
Cdd:cd03242 233 DAIEGRVQTfVTTTDLAdfDALWLRRAQIFRVDAGTLS 270
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-76 |
5.18e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 54.24 E-value: 5.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYIL---SLGRSFRTSRLTEAIRFGSSHFFIEAVFSQ 76
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLlgpSSSRKFDEEDFYLGDDPDLPEIEIELTFGS 79
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-77 |
4.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYI---LSLGRSFRTSRLTEAIRFGSSHFFIEAVFSQN 77
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVglyWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKN 80
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-77 |
2.11e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 2.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497916067 2 RVHSLFLKDFRNY-SELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSFRTSRLT-EAIRFGSSHFFIEAVFSQN 77
Cdd:COG0419 1 KLLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRsDLINVGSEEASVELEFEHG 78
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-172 |
2.64e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 3 VHSLFLKDFRNYSE-LRLELGPEMNSIFGLNAQGKTNILEA-LYILSL--GRSFRTSRLTEAIRFGSSHF----FIEAVF 74
Cdd:pfam02463 2 LKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAiLFVLGErsAKSLRSERLSDLIHSKSGAFvnsaEVEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 75 --SQNQVFH-----TLSIQVDKRGK-KILFDGAPITKlSALVGLFPVILFSVKDTTIIEGSPAERRrfldllLAQASEKY 146
Cdd:pfam02463 82 dnEDHELPIdkeevSIRRRVYRGGDsEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEI------IAMMKPER 154
|
170 180 190
....*....|....*....|....*....|...
gi 497916067 147 TGQI------ALYHKALDQRNAA-IKTQDYKTI 172
Cdd:pfam02463 155 RLEIeeeaagSRLKRKKKEALKKlIEETENLAE 187
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-170 |
7.75e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 45.95 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 6 LFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEAL-YIL-----SLGRSFRTSRLTEAIRFGSSH---FFIEAVFSQ 76
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIkLALygktsRLKRKSGGGFVKGDIRIGLEGkgkAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 77 NQVFHTLSIQVD-----KRGKKILFDGAPITKLSALVGLFPVILFSVKDT-TIIEGSPAERR-RFLDLLLAQASEKYTGQ 149
Cdd:pfam13476 81 NDGRYTYAIERSrelskKKGKTKKKEILEILEIDELQQFISELLKSDKIIlPLLVFLGQEREeEFERKEKKERLEELEKA 160
|
170 180
....*....|....*....|.
gi 497916067 150 IALYHKALDQRNAAIKTQDYK 170
Cdd:pfam13476 161 LEEKEDEKKLLEKLLQLKEKK 181
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-144 |
1.64e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.46 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 2 RVHSLFLKDFRNYSELRLELGPeMNSIFGLNAQGKTNILEALYILslgRSFRTSRLTEAI--------------RFGSSH 67
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFL---SDAARGGLQDALarrggleellwrgpRTITEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 68 FFIEAVFSQNQVF---HTLSIQVDKRGKKILFDGAPItKLSALVGLFPVILFSVKDTTiIEGSPAERRRFlDLLLAQASE 144
Cdd:COG4637 77 IRLELEFAEEDERdlrYELELGLPEPGGRPEVKEERL-WLKRGSGGRPFLDFRPKGRA-VGGEPERLDSP-ESLLSQLGD 153
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-269 |
6.86e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 44.51 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILslgrsFRTSRLTEAIRFGSSHFFIEAVFSQNQVF 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF-----LNNKEKFFEDDFLVLYLKDVIKIDKEDLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 81 HTLSIQVDKRGK------KILFDGAPITKlsalVGLFPVILFSVKDTTIIEGSPAERRRFLDLLLAQASEKYT---GQIA 151
Cdd:pfam13175 76 IFENISFSIDIEidveflLILFGYLEIKK----KYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYlkqFKIY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 152 LYHKALDQRNAAIKTQDYKTIAAWNSPLIAYGSLVALLRY-ECAKKLHKIFQNLWDNTLKETLSLRYESSLIttesPTLN 230
Cdd:pfam13175 152 IYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDkEDLKKLINELEKSINYHENVLENLQIKKLLI----SADR 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 497916067 231 DIASNYYEQLRLANTKDFELGYTTVGPHRDELIITLNDL 269
Cdd:pfam13175 228 NASDEDSEKINSLLGALKQRIFEEALQEELELTEKLKET 266
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-139 |
9.13e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALYILSLGRSfRTSRLTEAIRFGSSHFFIEAVFSQNQVF 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK-RTEKIEDMIKKGKNNLEVELEFRIGGHV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 81 HTLSIQVDKRGK------KILFDGAPITK---------------LSALVGLFPVILFSVKDTTIIEGSPAERRRFLDLLL 139
Cdd:PRK01156 80 YQIRRSIERRGKgsrreaYIKKDGSIIAEgfddttkyieknilgISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEIL 159
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
4-90 |
1.57e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.11 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 4 HSLFLKDFRNYS-ELRLELGPE------MNSIFGLNAQGKTNILEALYILS---LGRSFRTSRLTEAIRFGSSHF----F 69
Cdd:COG1106 3 ISFSIENFRSFKdELTLSMVASglrllrVNLIYGANASGKSNLLEALYFLRnlvLNSSQPGDKLVEPFLLDSESKnepsE 82
|
90 100
....*....|....*....|.
gi 497916067 70 IEAVFSQNQVFHTLSIQVDKR 90
Cdd:COG1106 83 FEILFLLDGVRYEYGFELDKE 103
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-61 |
1.45e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 39.97 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497916067 1 MRVHSLFLKDFRNYSElRLELG---PEMNSIFGLNAQGKTNILEA----LYILSLGRsFRTSRLTEAI 61
Cdd:cd03273 1 MHIKEIILDGFKSYAT-RTVISgfdPQFNAITGLNGSGKSNILDAicfvLGITNLST-VRASNLQDLI 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-43 |
1.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 497916067 1 MRVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEAL 43
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFI 43
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-88 |
5.93e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 37.58 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497916067 2 RVHSLFLKDFRNYSELRLELGPEMNSIFGLNAQGKTNILEALyILSLGRSF----RTSRLTEAIRFGSSHFFIEAVFsQN 77
Cdd:cd03277 2 SIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAI-CLGLGGKPkllgRAKKVGEFVKRGCDEGTIEIEL-YG 79
|
90
....*....|.
gi 497916067 78 QVFHtlsIQVD 88
Cdd:cd03277 80 NPGN---IQVD 87
|
|
| |
