|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-358 |
2.76e-161 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 455.77 E-value: 2.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFmTSDQF 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRV-EKGGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 81 ELPIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNK 160
Cdd:PRK00064 80 ELPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 161 QRNALLKTAtNYRELSYWDQELARLAESISQWRATYVEQLKEVAEEICATFLPEFEI-KINYYRGWDKD-----TPYAEI 234
Cdd:PRK00064 160 QRNALLKQA-DYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELaSLSYQSSVEDDaekieEDLLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 235 LEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRR 314
Cdd:PRK00064 239 LAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGRR 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515674915 315 ARLAECLKATKAQVFVSSITADQIADMHdENSRMFHVEHGKIEQ 358
Cdd:PRK00064 319 AALLERLKGLGAQVFITTTDLEDLADLL-ENAKIFHVEQGKITD 361
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-356 |
1.03e-142 |
|
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: 408.67 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFMTSDQ- 79
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 80 -FELPIGINKQRDGTTEVKISGQTgqKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRL 158
Cdd:TIGR00611 81 vTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 159 NKQRNALLKTATNYR----ELSYWDQELARLAESISQWRATYVEQLKEVAEEICATFLPEFEIKINYYRG--WDKDTPYA 232
Cdd:TIGR00611 159 LKQRNAALKQAQRQYgdrtTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 233 EILEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQ 312
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 515674915 313 RRARLAECLKATKAQVFVSSITADQIADMHDENS---RMFHVEHGKI 356
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRvtiALVSVDRGTI 365
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-344 |
5.15e-136 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 391.05 E-value: 5.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFmTSDQFEL 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEV-ERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 83 PIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNKQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 163 NALLKTA--TNYRELSYWDQELARLAESISQWRATYVEQLKEVAEEICATF-LPEFEIKINYYRGWDKDTP-----YAEI 234
Cdd:COG1195 161 NALLKQGreADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALsGGKEELELRYRSGWLYESAeleeaLLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 235 LEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRR 314
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 515674915 315 ARLAECLKATKAQVFVSSITADQIADMHDE 344
Cdd:COG1195 321 EALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-357 |
4.28e-34 |
|
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: 126.64 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFMtSDQFEL 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLE-RQGGEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 83 PIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNKQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 163 NALLKtatnyrelsywdqelarlaesisqwratyveqlkevaeeicatflpefeikinyyrgwdkdtpyaeileknferd 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 243 qqlgytfsGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRRARLAECLK 322
Cdd:cd03242 165 --------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAIE 236
|
330 340 350
....*....|....*....|....*....|....*
gi 515674915 323 AtKAQVFVSSITADQIADMHDENSRMFHVEHGKIE 357
Cdd:cd03242 237 G-RVQTFVTTTDLADFDALWLRRAQIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-212 |
4.76e-21 |
|
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: 94.65 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNI-EACDIQPSSGFNFLIGANGSGKTSILEAV-YLLG--HGRSFKSSLTGRIIQ-------NECS-ELFV 70
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGerSAKSLRSERLSDLIHsksgafvNSAEvEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 71 H--GRFMTSDQFELPIGINKQRDGTTEVKISGQTGQKlAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGF 148
Cdd:pfam02463 82 DneDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674915 149 YDAWGRVKRLNKQRNALLKTATNYRELSYWDQELARLAESISQWRAT-----YVEQLKEVAEEICATFL 212
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYL 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-358 |
2.76e-161 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 455.77 E-value: 2.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFmTSDQF 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRV-EKGGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 81 ELPIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNK 160
Cdd:PRK00064 80 ELPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 161 QRNALLKTAtNYRELSYWDQELARLAESISQWRATYVEQLKEVAEEICATFLPEFEI-KINYYRGWDKD-----TPYAEI 234
Cdd:PRK00064 160 QRNALLKQA-DYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELaSLSYQSSVEDDaekieEDLLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 235 LEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRR 314
Cdd:PRK00064 239 LAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGRR 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515674915 315 ARLAECLKATKAQVFVSSITADQIADMHdENSRMFHVEHGKIEQ 358
Cdd:PRK00064 319 AALLERLKGLGAQVFITTTDLEDLADLL-ENAKIFHVEQGKITD 361
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-356 |
1.03e-142 |
|
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: 408.67 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFMTSDQ- 79
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 80 -FELPIGINKQRDGTTEVKISGQTgqKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRL 158
Cdd:TIGR00611 81 vTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 159 NKQRNALLKTATNYR----ELSYWDQELARLAESISQWRATYVEQLKEVAEEICATFLPEFEIKINYYRG--WDKDTPYA 232
Cdd:TIGR00611 159 LKQRNAALKQAQRQYgdrtTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 233 EILEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQ 312
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 515674915 313 RRARLAECLKATKAQVFVSSITADQIADMHDENS---RMFHVEHGKI 356
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRvtiALVSVDRGTI 365
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-344 |
5.15e-136 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 391.05 E-value: 5.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFmTSDQFEL 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEV-ERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 83 PIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNKQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 163 NALLKTA--TNYRELSYWDQELARLAESISQWRATYVEQLKEVAEEICATF-LPEFEIKINYYRGWDKDTP-----YAEI 234
Cdd:COG1195 161 NALLKQGreADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALsGGKEELELRYRSGWLYESAeleeaLLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 235 LEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRR 314
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 515674915 315 ARLAECLKATKAQVFVSSITADQIADMHDE 344
Cdd:COG1195 321 EALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-317 |
4.64e-40 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 144.54 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNEcSELFVHGRFMTsdQF 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTGELPNGRLADLVRFGE-GEAWVHAEVET--GG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 81 ELPIGINKQRDGTTEVKISGQTGqKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNK 160
Cdd:PRK14079 78 GLSRLEVGLGPGRRELKLDGVRV-SLRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYERAVQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 161 QRNALLKTATNYrELSYWDQELARLAESISQWRATYVEQLKEVAEEICATFLPEFEIKINYYRGWDKDTpYAEILEKNFE 240
Cdd:PRK14079 157 QRNAALKSGGGW-GLHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRKPLRLELSESTAPEG-YLAALEARRA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515674915 241 RDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRRARL 317
Cdd:PRK14079 235 EELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELDPRRRGAL 311
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-357 |
4.28e-34 |
|
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: 126.64 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFMtSDQFEL 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLE-RQGGEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 83 PIGINKQRDGTTEVKISGQTGQKLAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGFYDAWGRVKRLNKQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 163 NALLKtatnyrelsywdqelarlaesisqwratyveqlkevaeeicatflpefeikinyyrgwdkdtpyaeileknferd 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 243 qqlgytfsGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAQGQHLTQMTGKQCIYLIDDFASELDSQRRARLAECLK 322
Cdd:cd03242 165 --------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAIE 236
|
330 340 350
....*....|....*....|....*....|....*
gi 515674915 323 AtKAQVFVSSITADQIADMHDENSRMFHVEHGKIE 357
Cdd:cd03242 237 G-RVQTFVTTTDLADFDALWLRRAQIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-212 |
4.76e-21 |
|
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: 94.65 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNI-EACDIQPSSGFNFLIGANGSGKTSILEAV-YLLG--HGRSFKSSLTGRIIQ-------NECS-ELFV 70
Cdd:pfam02463 2 LKRIEIEGFKSYaKTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGerSAKSLRSERLSDLIHsksgafvNSAEvEITF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 71 H--GRFMTSDQFELPIGINKQRDGTTEVKISGQTGQKlAQLAQVLPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSESGF 148
Cdd:pfam02463 82 DneDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTK-KEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674915 149 YDAWGRVKRLNKQRNALLKTATNYRELSYWDQELARLAESISQWRAT-----YVEQLKEVAEEICATFL 212
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYL 229
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
154-357 |
3.18e-19 |
|
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: 89.26 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 154 RVKRLNKQRNALLKTATNYRELSYWDQELARLAESISQ-WRATYVEQLKEVAEEICATFLPEFEIKINYYRGWDKDTPYA 232
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKErLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 233 EILEKNFERDQQLGYTFSGPNKADLKIKVNGTPVEDVLSRGQLKLMVCALRVAqgqhlTQMTGKQCIYLIDDFASELDSQ 312
Cdd:pfam02463 1041 ELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFA-----IQKYKPAPFYLLDEIDAALDDQ 1115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515674915 313 RRARLAECLKA--TKAQVFVSSITADQIADMhDENSRMFHVEHGKIE 357
Cdd:pfam02463 1116 NVSRVANLLKElsKNAQFIVISLREEMLEKA-DKLVGVTMVENGVST 1161
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-46 |
1.33e-11 |
|
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: 65.02 E-value: 1.33e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLL 46
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLL 46
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-332 |
5.17e-09 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 56.63 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 25 FNFLIGANGSGKTSILEAVYLLGHGRSFKSSLTGRIIQNECSELFVHGRFMTSDQFELPIGINKQRdgTTEVKISGQTGQ 104
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFL--EDGVRYRYGLDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 105 KLAQLAQVLPlQLIHPEGFDLLtdgpKHRRAFIDWGVFHSESGFYDAWGRVKRLNKQRNALLKTATNYRELSYWDQELAR 184
Cdd:pfam13304 79 EREDVEEKLS-SKPTLLEKRLL----LREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 185 LAESISQWRATYVEQLKEVAEEICATFLPEFeIKInYYRGWDKDTPYAEILEKnFERDQQLGYTFSGPNKADLKIKVNGT 264
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKEL-LQR-LVRGLKLADLNLSDLGE-GIEKSLLVDDRLRERGLILLENGGGG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515674915 265 PVE-DVLSRGQLKLmvcaLRVAQGQHLTQMTGKqcIYLIDDFASELDSQRRARLAECLKATK---AQVFVSS 332
Cdd:pfam13304 231 ELPaFELSDGTKRL----LALLAALLSALPKGG--LLLIDEPESGLHPKLLRRLLELLKELSrngAQLILTT 296
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-46 |
2.26e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 54.62 E-value: 2.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 515674915 1 MPLSRLIVKQFRNIEACDI--QPSSGFNFLIGANGSGKTSILEAVYLL 46
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTLLEAIALA 48
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-46 |
2.35e-08 |
|
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: 55.30 E-value: 2.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLL 46
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-48 |
3.06e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 54.94 E-value: 3.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515674915 3 LSRLIVKQFRNIEACDIQPSsGFNFLIGANGSGKTSILEAVYLLGH 48
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLG-PLTVLIGANGSGKSNLLDALRFLSD 46
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-148 |
4.74e-07 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins 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 that contain 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 50.66 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKSsltgrIIQNECSELFVHGRFMTSDQ--- 79
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASAD-----LIRSGAEKAVVEGVFDISDEeea 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 80 ------------FELPIGINKQRDGTTEVKISGQ--TGQKLAQLAQvlPLQLIHPEGFDLLTDGPKHRRAFIDWGVFHSE 145
Cdd:cd03241 76 kalllelgieddDDLIIRREISRKGRSRYFINGQsvTLKLLRELGS--LLVDIHGQHDHQNLLNPERQLDLLDGGLDDVE 153
|
...
gi 515674915 146 SGF 148
Cdd:cd03241 154 FLF 156
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-50 |
1.87e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYL---LGHGR 50
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVglyWGHGS 53
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-70 |
2.60e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 2.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 3 LSRLIVKQFRNI-EACDIQPSSGFNFLIGANGSGKTSILEAV-YLLGHGRSFKSSLTGRIIQNECSELFV 70
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIrYALYGKARSRSKLRSDLINVGSEEASV 71
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-43 |
3.30e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.02 E-value: 3.30e-05
10 20 30
....*....|....*....|....*....|....*...
gi 515674915 6 LIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAV 43
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAI 38
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-70 |
7.83e-05 |
|
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: 43.35 E-value: 7.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515674915 5 RLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVYLlghGRSFKSSLTGR------IIQNECSELFV 70
Cdd:cd03277 5 RIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICL---GLGGKPKLLGRakkvgeFVKRGCDEGTI 73
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-46 |
1.08e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.49 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 515674915 3 LSRLIVKQFRNIE-------ACDIQPSSGFNFLIGANGSGKTSILEAVYLL 46
Cdd:COG1106 2 LISFSIENFRSFKdeltlsmVASGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-63 |
4.37e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 4.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515674915 3 LSRLIVKQFRNI-EACDIQPSSGFNFLIGANGSGKTSILEAVyllghgrsfKSSLTGRIIQN 63
Cdd:cd03240 1 IDKLSIRNIRSFhERSEIEFFSPLTLIVGQNGAGKTTIIEAL---------KYALTGELPPN 53
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
21-147 |
4.84e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 40.37 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 21 PSSGFNFLIGANGSGKTSILEAVYLLGHGRSFKssltgriiQNECSELFVHGRFMTSDQFELPIGINKQR------DGTT 94
Cdd:cd03239 20 GSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAK--------LRRGSLLFLAGGGVKAGINSASVEITFDKsyflvlQGKV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 515674915 95 EVKISGqtGQK-LAQLAQVLPLQLIHPEGFDLLTD-----GPKHRRAFIDWGVFHSESG 147
Cdd:cd03239 92 EQILSG--GEKsLSALALIFALQEIKPSPFYVLDEidaalDPTNRRRVSDMIKEMAKHT 148
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-138 |
5.75e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674915 5 RLIVKQFR-NIEACDIQPSSG-FNFLIGANGSGKTSILEAVyLLGHGRSFKSSLTGRIIQNECSELFVHGRFMTSDqfel 82
Cdd:cd03227 1 KIVLGRFPsYFVPNDVTFGEGsLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKAGCIVAAVSAELIFTR---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515674915 83 piginkqrdgtteVKISGqtGQK-LAQLAQVLPLQLIHPEGFDLL------TDgPKHRRAFID 138
Cdd:cd03227 76 -------------LQLSG--GEKeLSALALILALASLKPRPLYILdeidrgLD-PRDGQALAE 122
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-46 |
1.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 515674915 3 LSRLIVKQFRNIEACDIqPSSGFNFLIGANGSGKTSILEAVYLL 46
Cdd:COG4938 1 IKSISIKNFGPFKEAEL-ELKPLTLLIGPNGSGKSTLIQALLLL 43
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-53 |
9.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.96 E-value: 9.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515674915 1 MPLSRLIVKQFRNIEACDIQPSSGFNFLIGANGSGKTSILEAVY--LLGHGRSFK 53
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRfaLFTDKRTEK 55
|
|
| |
