|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-361 |
7.07e-146 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 416.87 E-value: 7.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGi 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 81 ASNLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALR 160
Cdd:PRK00064 80 ELPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 161 QRNSWLRHgkLDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVS-LDDLTLSYYRGWDKDR-----DLLE 234
Cdd:PRK00064 160 QRNALLKQ--ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPeFELASLSYQSSVEDDAekieeDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 235 VLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQH 314
Cdd:PRK00064 238 ALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15595201 315 RMALCRLLEDLGCQVFITCVDPQLLKDGWRTdtpVSMFHVEHGKVSQ 361
Cdd:PRK00064 318 RAALLERLKGLGAQVFITTTDLEDLADLLEN---AKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-345 |
4.71e-136 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 391.83 E-value: 4.71e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 3 LTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVmLANGIAS 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEV-ERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 83 NLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 163 NSWLRHGKLDPASQ-AAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELV-SLDDLTLSYYRGWDKD-----RDLLEV 235
Cdd:COG1195 161 NALLKQGREADLALlDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSgGKEELELRYRSGWLYEsaeleEALLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 236 LASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHR 315
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 15595201 316 MALCRLLEDLGCQVFITCVDPQLLKDGWRT 345
Cdd:COG1195 321 EALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-359 |
1.35e-128 |
|
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: 373.23 E-value: 1.35e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVM--LAN 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSkgDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 79 GIASNLGISRERQGEFTIRIDGQNarSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKA 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 159 LRQRNSWLRHG---KLDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVSLDDLTLSYYRG--WDKDRDLL 233
Cdd:TIGR00611 159 LKQRNAALKQAqrqYGDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 234 EVLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQ 313
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15595201 314 HRMALCRLLEDLGCQVFITCVDPQLLKDGWRTDTP-VSMFHVEHGKV 359
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVtIALVSVDRGTI 365
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-360 |
1.42e-40 |
|
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: 143.98 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 3 LTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGiAS 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGG-EL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 83 NLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 163 NSWLRhgkldpasqaawdrelslasdeidayrrsyiqalkpvfeetlaelvslddltlsyyrgwdkdrdllevlassllr 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 243 dqqmghtqaGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHRMALCRLL 322
Cdd:cd03242 165 ---------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAI 235
|
330 340 350
....*....|....*....|....*....|....*...
gi 15595201 323 EDLGcQVFITCVDPQLLKDGWRTDTpvSMFHVEHGKVS 360
Cdd:cd03242 236 EGRV-QTFVTTTDLADFDALWLRRA--QIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
15-210 |
7.46e-28 |
|
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: 115.45 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 15 HPVTLSPSPRINILYGDNGSGKTSVLEAI-HLLGL--ARSFRSARLQPVIQYEEAACTVFGQVML--------ANGIASN 83
Cdd:pfam02463 15 KTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGErsAKSLRSERLSDLIHSKSGAFVNSAEVEItfdnedheLPIDKEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 84 LGISR--ERQGEFTIRIDGQNARSAAqLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQ 161
Cdd:pfam02463 95 VSIRRrvYRGGDSEYYINGKNVTKKE-VAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15595201 162 RNSWLRHGKLDPASQAAWDREL-----SLASDEIDAYRRSYIQALKPVFEETLA 210
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELklqelKLKEQAKKALEYYQLKEKLELEEEYLL 227
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-361 |
7.07e-146 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 416.87 E-value: 7.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGi 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 81 ASNLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALR 160
Cdd:PRK00064 80 ELPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 161 QRNSWLRHgkLDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVS-LDDLTLSYYRGWDKDR-----DLLE 234
Cdd:PRK00064 160 QRNALLKQ--ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPeFELASLSYQSSVEDDAekieeDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 235 VLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQH 314
Cdd:PRK00064 238 ALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15595201 315 RMALCRLLEDLGCQVFITCVDPQLLKDGWRTdtpVSMFHVEHGKVSQ 361
Cdd:PRK00064 318 RAALLERLKGLGAQVFITTTDLEDLADLLEN---AKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-345 |
4.71e-136 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 391.83 E-value: 4.71e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 3 LTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVmLANGIAS 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEV-ERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 83 NLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 163 NSWLRHGKLDPASQ-AAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELV-SLDDLTLSYYRGWDKD-----RDLLEV 235
Cdd:COG1195 161 NALLKQGREADLALlDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSgGKEELELRYRSGWLYEsaeleEALLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 236 LASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHR 315
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 15595201 316 MALCRLLEDLGCQVFITCVDPQLLKDGWRT 345
Cdd:COG1195 321 EALLELLADLGGQVFITTTDPEDFPALLER 350
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-359 |
1.35e-128 |
|
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: 373.23 E-value: 1.35e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVM--LAN 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSkgDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 79 GIASNLGISRERQGEFTIRIDGQNarSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKA 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 159 LRQRNSWLRHG---KLDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVSLDDLTLSYYRG--WDKDRDLL 233
Cdd:TIGR00611 159 LKQRNAALKQAqrqYGDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 234 EVLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQ 313
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15595201 314 HRMALCRLLEDLGCQVFITCVDPQLLKDGWRTDTP-VSMFHVEHGKV 359
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVtIALVSVDRGTI 365
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-318 |
5.56e-44 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 155.33 E-value: 5.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLlGLARSFRSARLQPVIQYEEAACTVFGQVMLANGI 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYL-ALTGELPNGRLADLVRFGEGEAWVHAEVETGGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 81 AS-NLGISRERQgefTIRIDGQNARsAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKAL 159
Cdd:PRK14079 80 SRlEVGLGPGRR---ELKLDGVRVS-LRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYERAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 160 RQRNSWLRHGklDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVSLDDLTLSYYRGWDKDRdLLEVLASS 239
Cdd:PRK14079 156 QQRNAALKSG--GGWGLHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRKPLRLELSESTAPEG-YLAALEAR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595201 240 LLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHRMAL 318
Cdd:PRK14079 233 RAEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELDPRRRGAL 311
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-360 |
1.42e-40 |
|
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: 143.98 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 3 LTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGiAS 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGG-EL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 83 NLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 163 NSWLRhgkldpasqaawdrelslasdeidayrrsyiqalkpvfeetlaelvslddltlsyyrgwdkdrdllevlassllr 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 243 dqqmghtqaGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHRMALCRLL 322
Cdd:cd03242 165 ---------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAI 235
|
330 340 350
....*....|....*....|....*....|....*...
gi 15595201 323 EDLGcQVFITCVDPQLLKDGWRTDTpvSMFHVEHGKVS 360
Cdd:cd03242 236 EGRV-QTFVTTTDLADFDALWLRRA--QIFRVDAGTLS 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
15-210 |
7.46e-28 |
|
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: 115.45 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 15 HPVTLSPSPRINILYGDNGSGKTSVLEAI-HLLGL--ARSFRSARLQPVIQYEEAACTVFGQVML--------ANGIASN 83
Cdd:pfam02463 15 KTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGErsAKSLRSERLSDLIHSKSGAFVNSAEVEItfdnedheLPIDKEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 84 LGISR--ERQGEFTIRIDGQNARSAAqLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQ 161
Cdd:pfam02463 95 VSIRRrvYRGGDSEYYINGKNVTKKE-VAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15595201 162 RNSWLRHGKLDPASQAAWDREL-----SLASDEIDAYRRSYIQALKPVFEETLA 210
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELklqelKLKEQAKKALEYYQLKEKLELEEEYLL 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
197-360 |
1.28e-15 |
|
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: 78.47 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 197 YIQALKPVFEETLAELVSLDDLTLSYYRGWDKDRDLLEVLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQ 276
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 277 KLVVCALRIAqghlINRAKRgQCVYLVDDLPSELDEQHRMALCRLLEDLG--CQVFITCVDPQLLKDGwrtDTPVSMFHV 354
Cdd:pfam02463 1084 TLVALALIFA----IQKYKP-APFYLLDEIDAALDDQNVSRVANLLKELSknAQFIVISLREEMLEKA---DKLVGVTMV 1155
|
....*.
gi 15595201 355 EHGKVS 360
Cdd:pfam02463 1156 ENGVST 1161
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-46 |
1.95e-09 |
|
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: 58.48 E-value: 1.95e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLL 46
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLL 46
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-61 |
5.72e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 56.54 E-value: 5.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595201 1 MSLTRVSVTAVRNL--HPVTLSPSPRINILYGDNGSGKTSVLEAI--HLLGLARSFRSARLQPVI 61
Cdd:COG3950 1 MRIKSLTIENFRGFedLEIDFDNPPRLTVLVGENGSGKTTLLEAIalALSGLLSRLDDVKFRKLL 65
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-339 |
5.84e-07 |
|
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: 50.47 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 25 INILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGIASNLGISRERQGE--FTIRIDGQN 102
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGvrYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 103 ARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDW---GVFHVEPRFLPVWQRLQKALRQRNSWLRHGKLDPASqaaW 179
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEElrlGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLL---L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 180 DRELSLA-SDEIDAYRRSYIQALKPVFEETLaeLVSLDDLTLSYYRGWDKDRDLLEVlaSSLLRDQQMGHTQAGpQRADL 258
Cdd:pfam13304 158 DEGLLLEdWAVLDLAADLALFPDLKELLQRL--VRGLKLADLNLSDLGEGIEKSLLV--DDRLRERGLILLENG-GGGEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 259 RIRLaghnaaeiLSRGQQKLvvcaLRIAqGHLINRAKRGQcVYLVDDLPSELDEQHRMALCRLLEDL---GCQVFITCVD 335
Cdd:pfam13304 233 PAFE--------LSDGTKRL----LALL-AALLSALPKGG-LLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHS 298
|
....
gi 15595201 336 PQLL 339
Cdd:pfam13304 299 PLLL 302
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
11-45 |
3.45e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.11 E-value: 3.45e-06
10 20 30
....*....|....*....|....*....|....*
gi 15595201 11 VRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHL 45
Cdd:pfam13476 6 FRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKL 40
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
15-46 |
6.03e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 47.73 E-value: 6.03e-06
10 20 30
....*....|....*....|....*....|....*...
gi 15595201 15 HPVTLS------PSPRINILYGDNGSGKTSVLEAIHLL 46
Cdd:COG1106 15 DELTLSmvasglRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-126 |
1.47e-05 |
|
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: 44.66 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 21 PSPRINILYGDNGSGKTSVLEAIHL-LGLARSFRSARLQPVIQYEEAACTVFGQVMLangiasnLGISrerQGEftirid 99
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIGLaLGGAQSATRRRSGVKAGCIVAAVSAELIFTR-------LQLS---GGE------ 82
|
90 100
....*....|....*....|....*..
gi 15595201 100 gqnaRSAAQLAETLPLQLINPDSFRLL 126
Cdd:cd03227 83 ----KELSALALILALASLKPRPLYIL 105
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-47 |
1.86e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.08 E-value: 1.86e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15595201 3 LTRVSVTAVRNLHPVTLSPSPrINILYGDNGSGKTSVLEAIHLLG 47
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFLS 45
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
7-43 |
8.65e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 8.65e-05
10 20 30
....*....|....*....|....*....|....*..
gi 15595201 7 SVTAVRNLHPvtLSPSPRINILYGDNGSGKTSVLEAI 43
Cdd:COG3910 23 NLPAVRNLEG--LEFHPPVTFFVGENGSGKSTLLEAI 57
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-46 |
1.44e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 1.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15595201 3 LTRVSVTAVR-NLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLL 46
Cdd:COG0419 2 LLRLRLENFRsYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYA 46
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
18-111 |
4.07e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 42.42 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595201 18 TLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACT----VFGQvmlaNGIASNLGISRERQGE 93
Cdd:COG4694 19 WLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNpsvrVFNR----DFVEENLRSGEEIKGI 94
|
90
....*....|....*...
gi 15595201 94 FTirIDGQNARSAAQLAE 111
Cdd:COG4694 95 FT--LGEENIELEEEIEE 110
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
16-49 |
1.61e-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: 39.50 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....
gi 15595201 16 PVTLSPSPRINILYGDNGSGKTSVLEAIhLLGLA 49
Cdd:cd03277 16 ETEFRPGPSLNMIIGPNGSGKSSIVCAI-CLGLG 48
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-46 |
3.21e-03 |
|
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: 39.12 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLL 46
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-50 |
5.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 5.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15595201 1 MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLAR 50
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLER 50
|
|
| |
