|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-361 |
7.89e-138 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 396.45 E-value: 7.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 1 MSLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQLSDGR 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 81 LSnLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALK 160
Cdd:PRK00064 81 LP-LGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 161 QRNSWLRrgTLDPVSQAAWDRELCLASDEIDSYRRSYIQQLKPVFERTLSELV-ELQGLTLSYYRGWDK-----ERPLSE 234
Cdd:PRK00064 160 QRNALLK--QADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISpEFELASLSYQSSVEDdaekiEEDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 235 VLTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQH 314
Cdd:PRK00064 238 ALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1914364368 315 RRALCRLLEDLNCQVFITCVDHELLSDGWQTdtpVSMFHVEHGRITQ 361
Cdd:PRK00064 318 RAALLERLKGLGAQVFITTTDLEDLADLLEN---AKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-345 |
6.45e-127 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 368.33 E-value: 6.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 3 LTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQlSDGRLS 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVE-RDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 83 NLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 163 NSWLRRG-TLDPVSQAAWDRELCLASDEIDSYRRSYIQQLKPVFERTLSELV-ELQGLTLSYYRGWDK-----ERPLSEV 235
Cdd:COG1195 161 NALLKQGrEADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSgGKEELELRYRSGWLYesaelEEALLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 236 LTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQHR 315
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 1914364368 316 RALCRLLEDLNCQVFITCVDHELLSDGWQT 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 |
1.55e-121 |
|
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: 355.12 E-value: 1.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 1 MSLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQLSD-- 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 79 GRLSNLGVSRDRQGEFQIRIDGQNarSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKA 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 159 LKQRNSWLRRGTLDPVSQAA---WDRELCLASDEIDSYRRSYIQQLKPVFERTLSELVELQGLTLSYYRG--WDKERPLS 233
Cdd:TIGR00611 159 LKQRNAALKQAQRQYGDRTTlevWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 234 EVLTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQ 313
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1914364368 314 HRRALCRLLEDLNCQVFITCVDHELLSDGWQTDTP-VSMFHVEHGRI 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 |
3.84e-39 |
|
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: 140.13 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 3 LTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQlSDGRLS 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLE-RQGGEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 83 NLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 163 NSWLRrgtldpvsqaawdrelclasdeidsyrrsyiqqlkpvfertlselvelqgltlsyyrgwdkerplsevltssllr 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 243 dqqightqsGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQHRRALCRLL 322
Cdd:cd03242 165 ---------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAI 235
|
330 340 350
....*....|....*....|....*....|....*...
gi 1914364368 323 EDLNcQVFITCVDHELLSDGWQTDTpvSMFHVEHGRIT 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 ... |
15-216 |
6.32e-27 |
|
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: 112.37 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 15 EPSTLLPSPRINVLYGDNGSGKTSVLEGI-HLLGL--ARSFRSARLLPVIQYEQQVCTLFGQVQL----SDGRL----SN 83
Cdd:pfam02463 15 KTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGErsAKSLRSERLSDLIHSKSGAFVNSAEVEItfdnEDHELpidkEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 84 LGVSR--DRQGEFQIRIDGQNARSAAqLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQ 161
Cdd:pfam02463 95 VSIRRrvYRGGDSEYYINGKNVTKKE-VAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914364368 162 RNSWLRRGTLDPVSQAAWDRELCL--------ASDEIDSYRRSYIQQLKPVFERTLSELVELQ 216
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLqelklkeqAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-361 |
7.89e-138 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 396.45 E-value: 7.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 1 MSLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQLSDGR 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 81 LSnLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALK 160
Cdd:PRK00064 81 LP-LGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 161 QRNSWLRrgTLDPVSQAAWDRELCLASDEIDSYRRSYIQQLKPVFERTLSELV-ELQGLTLSYYRGWDK-----ERPLSE 234
Cdd:PRK00064 160 QRNALLK--QADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISpEFELASLSYQSSVEDdaekiEEDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 235 VLTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQH 314
Cdd:PRK00064 238 ALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASELDDGR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1914364368 315 RRALCRLLEDLNCQVFITCVDHELLSDGWQTdtpVSMFHVEHGRITQ 361
Cdd:PRK00064 318 RAALLERLKGLGAQVFITTTDLEDLADLLEN---AKIFHVEQGKITD 361
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-345 |
6.45e-127 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 368.33 E-value: 6.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 3 LTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQlSDGRLS 82
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVE-RDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 83 NLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQR 162
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 163 NSWLRRG-TLDPVSQAAWDRELCLASDEIDSYRRSYIQQLKPVFERTLSELV-ELQGLTLSYYRGWDK-----ERPLSEV 235
Cdd:COG1195 161 NALLKQGrEADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSgGKEELELRYRSGWLYesaelEEALLEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 236 LTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQHR 315
Cdd:COG1195 241 LAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERR 320
|
330 340 350
....*....|....*....|....*....|
gi 1914364368 316 RALCRLLEDLNCQVFITCVDHELLSDGWQT 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 |
1.55e-121 |
|
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: 355.12 E-value: 1.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 1 MSLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQLSD-- 78
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 79 GRLSNLGVSRDRQGEFQIRIDGQNarSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKA 158
Cdd:TIGR00611 81 VTIPLEGLLKKKGKKAKVNIDGQD--KLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 159 LKQRNSWLRRGTLDPVSQAA---WDRELCLASDEIDSYRRSYIQQLKPVFERTLSELVELQGLTLSYYRG--WDKERPLS 233
Cdd:TIGR00611 159 LKQRNAALKQAQRQYGDRTTlevWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGelWDKETDYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 234 EVLTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQ 313
Cdd:TIGR00611 239 EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1914364368 314 HRRALCRLLEDLNCQVFITCVDHELLSDGWQTDTP-VSMFHVEHGRI 359
Cdd:TIGR00611 319 RRRLLAELLQSLGVQVFVTAISLDHLKEMWDPNRVtIALVSVDRGTI 365
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-318 |
1.97e-40 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 145.70 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 1 MSLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLlGLARSFRSARLLPVIQYEQQVCTLFGQVQlSDGR 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYL-ALTGELPNGRLADLVRFGEGEAWVHAEVE-TGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 81 LSNLGVSRDRQGEfQIRIDGQNARsAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALK 160
Cdd:PRK14079 79 LSRLEVGLGPGRR-ELKLDGVRVS-LRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYERAVQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 161 QRNSWLRRGTlDPvSQAAWDRELCLASDEIDSYRRSYIQQLKPVFERTLSELVELQGLTLSYYRGWDKERPLSEvLTSSL 240
Cdd:PRK14079 157 QRNAALKSGG-GW-GLHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRKPLRLELSESTAPEGYLAA-LEARR 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914364368 241 LRDQQIGHTQSGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQHRRAL 318
Cdd:PRK14079 234 AEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELDPRRRGAL 311
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-360 |
3.84e-39 |
|
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: 140.13 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 3 LTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLLGLARSFRSARLLPVIQYEQQVCTLFGQVQlSDGRLS 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLE-RQGGEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 83 NLGVSRDRQGEFQIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQR 162
Cdd:cd03242 80 ALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 163 NSWLRrgtldpvsqaawdrelclasdeidsyrrsyiqqlkpvfertlselvelqgltlsyyrgwdkerplsevltssllr 242
Cdd:cd03242 160 NALLK--------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 243 dqqightqsGPQRADLRLRLGAHNAADILSRGQQKLVVCALRIAQGHLVDQAKRGQCIYLVDDLPSELDEQHRRALCRLL 322
Cdd:cd03242 165 ---------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAELDLGRQAALLDAI 235
|
330 340 350
....*....|....*....|....*....|....*...
gi 1914364368 323 EDLNcQVFITCVDHELLSDGWQTDTpvSMFHVEHGRIT 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 ... |
15-216 |
6.32e-27 |
|
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: 112.37 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 15 EPSTLLPSPRINVLYGDNGSGKTSVLEGI-HLLGL--ARSFRSARLLPVIQYEQQVCTLFGQVQL----SDGRL----SN 83
Cdd:pfam02463 15 KTVILPFSPGFTAIVGPNGSGKSNILDAIlFVLGErsAKSLRSERLSDLIHSKSGAFVNSAEVEItfdnEDHELpidkEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 84 LGVSR--DRQGEFQIRIDGQNARSAAqLAETLPLQLINPDSFRLLEGSPKIRRQFLDWGVFHVEHRFLPAWQRLQKALKQ 161
Cdd:pfam02463 95 VSIRRrvYRGGDSEYYINGKNVTKKE-VAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914364368 162 RNSWLRRGTLDPVSQAAWDRELCL--------ASDEIDSYRRSYIQQLKPVFERTLSELVELQ 216
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLqelklkeqAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
189-360 |
6.86e-14 |
|
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: 73.08 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 189 EIDSYRRSYIQQLKPVFERTLSELVELQGLTLSYYRGWDKERPLSEVLTSSLLRDQQIGHTQSGPQRADLRLRLGAHNAA 268
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNL 1075
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 269 DILSRGQQKLVVCALRIAQghlvdQAKRGQCIYLVDDLPSELDEQHRRALCRLLEDL--NCQVFITCVDHELLSDGwqtD 346
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFAI-----QKYKPAPFYLLDEIDAALDDQNVSRVANLLKELskNAQFIVISLREEMLEKA---D 1147
|
170
....*....|....
gi 1914364368 347 TPVSMFHVEHGRIT 360
Cdd:pfam02463 1148 KLVGVTMVENGVST 1161
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-46 |
1.84e-06 |
|
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: 49.23 E-value: 1.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1914364368 1 MSLTRI---NFtavRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHLL 46
Cdd:COG3593 1 MKLEKIkikNF---RSIKDLSIELSDDLTVLVGENNSGKSSILEALRLL 46
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-61 |
5.19e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 47.30 E-value: 5.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914364368 1 MSLTRI---NFTAVRNLEpSTLLPSPRINVLYGDNGSGKTSVLEGI--HLLGLARSFRSARLLPVI 61
Cdd:COG3950 1 MRIKSLtieNFRGFEDLE-IDFDNPPRLTVLVGENGSGKTTLLEAIalALSGLLSRLDDVKFRKLL 65
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-332 |
4.08e-05 |
|
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: 45.07 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 25 INVLYGDNGSGKTSVLEGIHLL-GLARSFRSARLLPVIQYEQQVCTlFGQVQLSDGRLSNLGVSRDRQGE--FQIRIDGQ 101
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLaDFDALVIGLTDERSRNGGIGGIP-SLLNGIDPKEPIEFEISEFLEDGvrYRYGLDLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 102 NARSAAQLAETLPLQLINPDSFRLLEGSPKIRRQFLDW---GVFHVEHRFLPAWQRLQKALKQRNSWLRRgTLDPVSQAA 178
Cdd:pfam13304 80 REDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEElrlGLDVEERIELSLSELSDLISGLLLLSIIS-PLSFLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 179 WDRELcLASDEIDSYRRSYIQQLKPVFERTLSELVELQGLTLSyyrgwDKERPLSEVLTSSLLRDQQIGHTQSGPQRADL 258
Cdd:pfam13304 159 EGLLL-EDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLS-----DLGEGIEKSLLVDDRLRERGLILLENGGGGEL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914364368 259 RLRLgahnaadiLSRGQQKLvvcaLRIAqGHLVDQAKRGQcIYLVDDLPSELDEQHRRALCRLLEDL---NCQVFIT 332
Cdd:pfam13304 233 PAFE--------LSDGTKRL----LALL-AALLSALPKGG-LLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILT 295
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
23-46 |
7.09e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 44.26 E-value: 7.09e-05
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-45 |
1.33e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.48 E-value: 1.33e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1914364368 7 NFtavRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIHL 45
Cdd:pfam13476 5 NF---RSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKL 40
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-47 |
1.75e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 1.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1914364368 3 LTRI---NFTAVRNLEpstlLPSPRINVLYGDNGSGKTSVLEGIHLLG 47
Cdd:COG4637 2 ITRIrikNFKSLRDLE----LPLGPLTVLIGANGSGKSNLLDALRFLS 45
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-126 |
3.17e-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: 40.81 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914364368 15 EPSTLLPSPRINVLYGDNGSGKTSVLEGIhLLGLARSFRSARLLPVIQYEQQVCTLFGQVQLSDGRLSnlgvsrdrQGEf 94
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQLS--------GGE- 82
|
90 100 110
....*....|....*....|....*....|..
gi 1914364368 95 qiridgqnaRSAAQLAETLPLQLINPDSFRLL 126
Cdd:cd03227 83 ---------KELSALALILALASLKPRPLYIL 105
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
10-43 |
8.00e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.52 E-value: 8.00e-04
10 20 30
....*....|....*....|....*....|....
gi 1914364368 10 AVRNLEPstLLPSPRINVLYGDNGSGKTSVLEGI 43
Cdd:COG3910 26 AVRNLEG--LEFHPPVTFFVGENGSGKSTLLEAI 57
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-46 |
1.40e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1914364368 3 LTRINFTAVRNLEPSTLLP-SPRINVLYGDNGSGKTSVLEGIHLL 46
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDfDDGLNLIVGPNGAGKSTILEAIRYA 46
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-55 |
1.80e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 40.10 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1914364368 3 LTRINftAVRNL----EPSTLLPSPRINVLYGDNGSGKTSvlegihllgLARSFRSA 55
Cdd:COG4694 2 ITKIK--KLKNVgafkDFGWLAFFKKLNLIYGENGSGKST---------LSRILRSL 47
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-49 |
3.42e-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: 38.35 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1914364368 2 SLTRINFTAVRNLEPSTLLPSPRINVLYGDNGSGKTSVLEGIhLLGLA 49
Cdd:cd03277 2 SIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAI-CLGLG 48
|
|
| |
