|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-373 |
2.26e-139 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 401.46 E-value: 2.26e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQ 160
Cdd:PRK00064 81 LPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 161 RNALLKHSNmalrrgygdddgasaLSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTLD 240
Cdd:PRK00064 161 RNALLKQAD---------------YAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELASLSYQSSVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 241 kavtelaggpsRDPAVFEAAMLTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLL 320
Cdd:PRK00064 226 -----------DDAEKIEEDLLEALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELL 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1091125400 321 -SSDGKDPVLILDDVFAELDAKRRERLVH-VAEEAEQVLITAAVGDDLPGNLDDA 373
Cdd:PRK00064 295 kEETGEAPILLLDDVASELDDGRRAALLErLKGLGAQVFITTTDLEDLADLLENA 349
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-373 |
1.63e-132 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 383.74 E-value: 1.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 2 HVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGREL 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 82 TTHLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQR 161
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 162 NALLKhsnmalrrgygdDDGASALSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTLDK 241
Cdd:COG1195 161 NALLK------------QGREADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 242 avtelaggpsrDPAVFEAAMLTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLLS 321
Cdd:COG1195 229 -----------ESAELEEALLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLK 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1091125400 322 SD-GKDPVLILDDVFAELDAKRRERLVH-VAEEAEQVLITAAVGDDLPGNLDDA 373
Cdd:COG1195 298 EEtGEAPILLLDDVFAELDEERREALLElLADLGGQVFITTTDPEDFPALLERA 351
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-371 |
2.43e-115 |
|
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: 340.49 E-value: 2.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPHGAN-QAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLR 159
Cdd:TIGR00611 81 VTIPLEGLLKKKGkKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 160 QRNALLKHsnmaLRRGYGDddgasaLSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTL 239
Cdd:TIGR00611 161 QRNAALKQ----AQRQYGD------RTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 240 DKAVTELAggpsrdpavfeaamlTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQL 319
Cdd:TIGR00611 231 WDKETDYA---------------EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGEL 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1091125400 320 LSSD-GKDPVLILDDVFAELDAKRRERLVHVAEEA-EQVLITAAVGDDLPGNLD 371
Cdd:TIGR00611 296 LREEgGEYPILLLDDVASELDDQRRRLLAELLQSLgVQVFVTAISLDHLKEMWD 349
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-371 |
1.60e-87 |
|
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: 266.09 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 3 VRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRELT 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 83 THLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQRN 162
Cdd:cd03242 81 LELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 163 ALLKhsnmalrrgygdddgasalstldvwdgqlahfgaqvvagrhglvdtlgpliaeayhsvapesrpasveyrstldka 242
Cdd:cd03242 161 ALLK---------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 243 vtelaggpsrdpavfeaamltelgrrrkeeidrgitlvGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLLSS 322
Cdd:cd03242 165 --------------------------------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKE 206
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1091125400 323 -DGKDPVLILDDVFAELDAKRRERLVHVAEEAEQVLITAAVGDDLPGNLD 371
Cdd:cd03242 207 vSGEYPVLLLDDVLAELDLGRQAALLDAIEGRVQTFVTTTDLADFDALWL 256
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-174 |
7.11e-12 |
|
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: 67.30 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 2 HVRELDLRDFRSWPE-LNLKLEPGVTVIAGRNGHGKTNIVEAVHYT---STLSSHRVSTDAPLVAS-NRPN---ARVSVT 73
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVlgeRSAKSLRSERLSDLIHSkSGAFvnsAEVEIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 74 TVNDGR-------ELTTHLLIKPHGANQAQINRtklKSAR--EILGVLSTVMFSPEDLRLINGEPA---------ERRRF 135
Cdd:pfam02463 81 FDNEDHelpidkeEVSIRRRVYRGGDSEYYING---KNVTkkEVAELLESQGISPEAYNFLVQGGKieiiammkpERRLE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091125400 136 LDDLAalrtprlggARADYERVLRQRNALLKHSNMALRR 174
Cdd:pfam02463 158 IEEEA---------AGSRLKRKKKEALKKLIEETENLAE 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-373 |
2.26e-139 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 401.46 E-value: 2.26e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQ 160
Cdd:PRK00064 81 LPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 161 RNALLKHSNmalrrgygdddgasaLSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTLD 240
Cdd:PRK00064 161 RNALLKQAD---------------YAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEISPEFELASLSYQSSVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 241 kavtelaggpsRDPAVFEAAMLTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLL 320
Cdd:PRK00064 226 -----------DDAEKIEEDLLEALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQKLLLLALKLAEAELL 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1091125400 321 -SSDGKDPVLILDDVFAELDAKRRERLVH-VAEEAEQVLITAAVGDDLPGNLDDA 373
Cdd:PRK00064 295 kEETGEAPILLLDDVASELDDGRRAALLErLKGLGAQVFITTTDLEDLADLLENA 349
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-373 |
1.63e-132 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 383.74 E-value: 1.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 2 HVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGREL 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 82 TTHLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQR 161
Cdd:COG1195 81 RLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 162 NALLKhsnmalrrgygdDDGASALSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTLDK 241
Cdd:COG1195 161 NALLK------------QGREADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 242 avtelaggpsrDPAVFEAAMLTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLLS 321
Cdd:COG1195 229 -----------ESAELEEALLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQQKSLVLALKLAQAELLK 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1091125400 322 SD-GKDPVLILDDVFAELDAKRRERLVH-VAEEAEQVLITAAVGDDLPGNLDDA 373
Cdd:COG1195 298 EEtGEAPILLLDDVFAELDEERREALLElLADLGGQVFITTTDPEDFPALLERA 351
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-371 |
2.43e-115 |
|
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: 340.49 E-value: 2.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPHGAN-QAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLR 159
Cdd:TIGR00611 81 VTIPLEGLLKKKGkKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSAWSDYQRVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 160 QRNALLKHsnmaLRRGYGDddgasaLSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYHSVAPESRPASVEYRSTL 239
Cdd:TIGR00611 161 QRNAALKQ----AQRQYGD------RTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQKAHQLLLPELESLSLFYRGEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 240 DKAVTELAggpsrdpavfeaamlTELGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQL 319
Cdd:TIGR00611 231 WDKETDYA---------------EALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQLRSLALALRLAEGEL 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1091125400 320 LSSD-GKDPVLILDDVFAELDAKRRERLVHVAEEA-EQVLITAAVGDDLPGNLD 371
Cdd:TIGR00611 296 LREEgGEYPILLLDDVASELDDQRRRLLAELLQSLgVQVFVTAISLDHLKEMWD 349
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-371 |
1.60e-87 |
|
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: 266.09 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 3 VRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRELT 82
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 83 THLLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQRN 162
Cdd:cd03242 81 LELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQKALRQRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 163 ALLKhsnmalrrgygdddgasalstldvwdgqlahfgaqvvagrhglvdtlgpliaeayhsvapesrpasveyrstldka 242
Cdd:cd03242 161 ALLK---------------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 243 vtelaggpsrdpavfeaamltelgrrrkeeidrgitlvGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLLSS 322
Cdd:cd03242 165 --------------------------------------GPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKE 206
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1091125400 323 -DGKDPVLILDDVFAELDAKRRERLVHVAEEAEQVLITAAVGDDLPGNLD 371
Cdd:cd03242 207 vSGEYPVLLLDDVLAELDLGRQAALLDAIEGRVQTFVTTTDLADFDALWL 256
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-359 |
3.52e-50 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 172.28 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTlSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALT-GELPNGRLADLVRFGEGEAWVHAEVETGGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPhGANQAQINRTKLkSAREILGVLSTVMFSPEDLRLINGEPAERRRFLDDLAALRTPRLGGARADYERVLRQ 160
Cdd:PRK14079 80 SRLEVGLGP-GRRELKLDGVRV-SLRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRLSARYAALLSAYERAVQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 161 RNALLKhsnmalrrgygdddgASALSTLDVWDGQLAHFGAQVVAGRHGLVDTLGPLIAEAYhsvapesrpASVEYRSTLD 240
Cdd:PRK14079 158 RNAALK---------------SGGGWGLHVWDDELVKLGDEIMALRRRALTRLSELAREAY---------AELGSRKPLR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 241 KAVTElaggpSRDPAVFEAAmlteLGRRRKEEIDRGITLVGPHRDDLALMLGDNPAKGYASHGETWSYALSLHLAEYQLL 320
Cdd:PRK14079 214 LELSE-----STAPEGYLAA----LEARRAEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAEHRLL 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1091125400 321 SSD-GKDPVLILDDVFAELDAKRRERLVHVAEEAEQVLIT 359
Cdd:PRK14079 285 WEHfGEAPVLLVDDFTAELDPRRRGALLALAASLPQAIVA 324
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-174 |
7.11e-12 |
|
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: 67.30 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 2 HVRELDLRDFRSWPE-LNLKLEPGVTVIAGRNGHGKTNIVEAVHYT---STLSSHRVSTDAPLVAS-NRPN---ARVSVT 73
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVlgeRSAKSLRSERLSDLIHSkSGAFvnsAEVEIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 74 TVNDGR-------ELTTHLLIKPHGANQAQINRtklKSAR--EILGVLSTVMFSPEDLRLINGEPA---------ERRRF 135
Cdd:pfam02463 81 FDNEDHelpidkeEVSIRRRVYRGGDSEYYING---KNVTkkEVAELLESQGISPEAYNFLVQGGKieiiammkpERRLE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091125400 136 LDDLAalrtprlggARADYERVLRQRNALLKHSNMALRR 174
Cdd:pfam02463 158 IEEEA---------AGSRLKRKKKEALKKLIEETENLAE 187
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-186 |
1.50e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.25 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 4 RELDLRDFRSW-PELNLKLEPGVTVIAGRNGHGKTNIVEAVH---YTSTLSSHRVSTDapLVASNRPNARVSVTTVNDGR 79
Cdd:COG0419 3 LRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRyalYGKARSRSKLRSD--LINVGSEEASVELEFEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 80 ELTthlLIKPHGanqaqinrtklksareilgvlstvmfspEDLRLINGEPAERRRFLDDLAALRTP-----RLGGARADY 154
Cdd:COG0419 81 RYR---IERRQG----------------------------EFAEFLEAKPSERKEALKRLLGLEIYeelkeRLKELEEAL 129
|
170 180 190
....*....|....*....|....*....|..
gi 1091125400 155 ERVLRQRNALLKHSNMALRRgYGDDDGASALS 186
Cdd:COG0419 130 ESALEELAELQKLKQEILAQ-LSGLDPIETLS 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-164 |
2.73e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRPNARVSVTTVNDGRE 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDVITIGAEEAEIELWFEHAGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 81 LTTHLLIKPHGANqAQINRTKLKSAREIL-GVLSTVMFSPEDLR-------------------LINGEPAERRRFLDDLA 140
Cdd:PRK02224 81 YHIERRVRLSGDR-ATTAKCVLETPEGTIdGARDVREEVTELLRmdaeafvncayvrqgevnkLINATPSDRQDMIDDLL 159
|
170 180 190
....*....|....*....|....*....|
gi 1091125400 141 ALRT-----PRLGGARADYERVLR-QRNAL 164
Cdd:PRK02224 160 QLGKleeyrERASDARLGVERVLSdQRGSL 189
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-122 |
1.14e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 51.73 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 6 LDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYTSTLSSHRVSTDAPLVASNRP---------NARVSVTTVN 76
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDiriglegkgKAYVEITFEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1091125400 77 DGRELTThlLIKPHGANQAQINRTKLKSAREILGVLSTVMFSPEDL 122
Cdd:pfam13476 81 NDGRYTY--AIERSRELSKKKGKTKKKEILEILEIDELQQFISELL 124
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-57 |
1.45e-07 |
|
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: 52.70 E-value: 1.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYT-STLSSHRVSTD 57
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLlGPSSSRKFDEE 58
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-82 |
1.58e-05 |
|
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: 45.29 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 3 VRELDLRDFRSWPELN-LKLEPGVTVIAGRNGHGKTNIVEAVHYTST----LSSHRVSTDAPLVASNRPNARVSVT-TVN 76
Cdd:cd03240 1 IDKLSIRNIRSFHERSeIEFFSPLTLIVGQNGAGKTTIIEALKYALTgelpPNSKGGAHDPKLIREGEVRAQVKLAfENA 80
|
....*.
gi 1091125400 77 DGRELT 82
Cdd:cd03240 81 NGKKYT 86
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-140 |
3.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 2 HVRELDLRDFRSW-PELNLKLEPGVTVIAGRNGHGKTNIVEAVHY---TSTLSSHRVSTDAPLVASNRPN-----ARVSV 72
Cdd:TIGR02169 1 YIERIELENFKSFgKKKVIPFSKGFTVISGPNGSGKSNIGDAILFalgLSSSKAMRAERLSDLISNGKNGqsgneAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 73 TTVNDGRELTTHLLI-------KPHGANQAQINRTKLkSAREILGVLSTVMFSPE--------DL-RLINGEPAERRRFL 136
Cdd:TIGR02169 81 TFKNDDGKFPDELEVvrrlkvtDDGKYSYYYLNGQRV-RLSEIHDFLAAAGIYPEgynvvlqgDVtDFISMSPVERRKII 159
|
....
gi 1091125400 137 DDLA 140
Cdd:TIGR02169 160 DEIA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-43 |
7.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAV 43
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAI 43
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-139 |
1.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHYtSTLSSHRVSTDAPLVASNRPNARVSV-------- 72
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRF-ALFTDKRTEKIEDMIKKGKNNLEVELefrigghv 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091125400 73 -----TTVNDGRELTTHLLIKPHGANQAQ-INRTKLKSAREILG----VLSTVMFSP--EDLRLINGEPAERRRFLDDL 139
Cdd:PRK01156 80 yqirrSIERRGKGSRREAYIKKDGSIIAEgFDDTTKYIEKNILGiskdVFLNSIFVGqgEMDSLISGDPAQRKKILDEI 158
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
5-43 |
2.59e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.68 E-value: 2.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1091125400 5 ELDLRDFRSWPE-LNLKLEPGVTVIAGRNGHGKTNIVEAV 43
Cdd:cd03278 3 KLELKGFKSFADkTTIPFPPGLTAIVGPNGSGKSNIIDAI 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-45 |
9.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 9.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEAVHY 45
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRA 45
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-80 |
2.73e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 39.20 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091125400 1 MHVRELDLRDFRSWPELN--LKLEPGVTVIAGRNGHGKTNIVEAVHYT---STLSSHRVSTDAPLVASNRPNARV--SVT 73
Cdd:cd03273 1 MHIKEIILDGFKSYATRTviSGFDPQFNAITGLNGSGKSNILDAICFVlgiTNLSTVRASNLQDLIYKRGQAGITkaSVT 80
|
....*..
gi 1091125400 74 TVNDGRE 80
Cdd:cd03273 81 IVFDNSD 87
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-42 |
3.27e-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: 39.50 E-value: 3.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1091125400 1 MHVRELDLRDFRSWPELNLKLEPGVTVIAGRNGHGKTNIVEA 42
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEA 42
|
|
| |
