|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
5-360 |
5.77e-138 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 396.45 E-value: 5.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLA 84
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGREL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 85 EFTTQFKRSSNR--RITEYNESKIAnnELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMH 162
Cdd:PRK00064 82 PLGLEIDKKGGRkvRINGEPQRKLA--ELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 163 ERNKILVEdiRDDNWLKIIEEKMADISNHIANNRLKTLEFMQQAIDD----LENEFPKADLSIDGIVEQkilnGKKNIVS 238
Cdd:PRK00064 160 QRNALLKQ--ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKthqeISPEFELASLSYQSSVED----DAEKIEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 239 FITAELYQTRSKDKLLGRTSFGVHKSDFLVKHQKkNILAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVH 318
Cdd:PRK00064 234 DLLEALAKNRERDRARGRTLVGPHRDDLRFRING-LPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502141139 319 LDDKRRQYLIEFLIGLNMQLWVTTTNLEGIENFATKAQLIKL 360
Cdd:PRK00064 313 LDDGRRAALLERLKGLGAQVFITTTDLEDLADLLENAKIFHV 354
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
5-356 |
3.08e-102 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 305.16 E-value: 3.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLA 84
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 85 EFTTQFKRSSNRRITeYNESKIANN-ELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMHE 163
Cdd:COG1195 81 RLGLGLSRGGKKRVR-INGKPVRRLsDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 164 RNKILvEDIR--DDNWLKIIEEKMADISNHIANNRLKTLEFMQQAIDDLENEFPKADLSIDGIVEQKILNGKKNIVSFIT 241
Cdd:COG1195 160 RNALL-KQGReaDLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLYESAELEEALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 242 AELYQTRSKDKLLGRTSFGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVHLDD 321
Cdd:COG1195 239 EALAENRERDLARGRTLVGPHRDDLEFTLNGKPA-KKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDE 317
|
330 340 350
....*....|....*....|....*....|....*
gi 502141139 322 KRRQYLIEFLIGLNMQLWVTTTNLEGIENFATKAQ 356
Cdd:COG1195 318 ERREALLELLADLGGQVFITTTDPEDFPALLERAK 352
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
6-358 |
4.22e-50 |
|
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: 168.63 E-value: 4.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 6 LHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLAE 85
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 86 FTTQFKRSSNRRIteynesKIANNELSKFTSM------VWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEY 159
Cdd:cd03242 81 LELTIRSGGGRKA------RLNGIKVRRLSDLlgvlnaVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 160 YMHERNKILVedirddnwlkiieekmadisnhiannrlktlefmqqaiddlenefpkadlsidgiveqkilngkknivsf 239
Cdd:cd03242 155 ALRQRNALLK---------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 240 itaelyqtrskdkllgrtsfGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVHL 319
Cdd:cd03242 165 --------------------GPHRDDLLFFLNDKPA-ADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAEL 223
|
330 340 350
....*....|....*....|....*....|....*....
gi 502141139 320 DDKRRQYLIEFLIGLnMQLWVTTTNLEGIENFATKAQLI 358
Cdd:cd03242 224 DLGRQAALLDAIEGR-VQTFVTTTDLADFDALWLRRAQI 261
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
5-348 |
7.79e-43 |
|
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: 152.51 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSK---- 80
Cdd:TIGR00611 2 YLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGdrev 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 81 -------LGLAEFTTQFKRSSNRRITEYNESkiannelskfTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAEL 153
Cdd:TIGR00611 82 tipleglLKKKGKKAKVNIDGQDKLSDLAGL----------LPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 154 VSKYEYYMHERNKILVEDIR---DDNWLKIIEEKMADISNHIANNRlktlefmQQAIDDLENEFPKAdlsidgivEQKIL 230
Cdd:TIGR00611 152 WSDYQRVLKQRNAALKQAQRqygDRTTLEVWDSQLAELGAKVSAWR-------AEFIEKLEPEAQKA--------HQLLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 231 NGKKNIVSF-----------ITAELYQTRSKDKLLGRTSFGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNY 299
Cdd:TIGR00611 217 PELESLSLFyrgelwdketdYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPV-EDFASQGQLRSLALALRLAEGEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502141139 300 AIKLTKIAPILLLDEVFVHLDDKRRQYLIEFLIGLNMQLWVTTTNLEGI 348
Cdd:TIGR00611 296 LREEGGEYPILLLDDVASELDDQRRRLLAELLQSLGVQVFVTAISLDHL 344
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-342 |
1.33e-06 |
|
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: 49.31 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 30 ILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHclvkallqsKLGLAEFTTQFKRSSNRRITEYNESKIANN 109
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIG---------GIPSLLNGIDPKEPIEFEISEFLEDGVRYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 110 ---ELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMHERNKILVEDIRDDNWLKIIEEKma 186
Cdd:pfam13304 74 yglDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 187 DISNHIANNRLKTLEFMQQAIDDLENEFPKADLsidgivEQKILNGKKNIVSFITAELYqtRSKDKLLGRTSFGVHKSDF 266
Cdd:pfam13304 152 SFLLLLDEGLLLEDWAVLDLAADLALFPDLKEL------LQRLVRGLKLADLNLSDLGE--GIEKSLLVDDRLRERGLIL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502141139 267 LVKHQKKNILAKFCSTGEQKAILIAIILAEMNyaikltKIAPILLLDEVFVHLDDKRRQYLIEFL---IGLNMQLWVTT 342
Cdd:pfam13304 224 LENGGGGELPAFELSDGTKRLLALLAALLSAL------PKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTT 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recF |
PRK00064 |
recombination protein F; Reviewed |
5-360 |
5.77e-138 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 396.45 E-value: 5.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLA 84
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVIHGRVEKGGREL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 85 EFTTQFKRSSNR--RITEYNESKIAnnELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMH 162
Cdd:PRK00064 82 PLGLEIDKKGGRkvRINGEPQRKLA--ELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLLFQIEPVYASALSQYERALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 163 ERNKILVEdiRDDNWLKIIEEKMADISNHIANNRLKTLEFMQQAIDD----LENEFPKADLSIDGIVEQkilnGKKNIVS 238
Cdd:PRK00064 160 QRNALLKQ--ADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKthqeISPEFELASLSYQSSVED----DAEKIEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 239 FITAELYQTRSKDKLLGRTSFGVHKSDFLVKHQKkNILAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVH 318
Cdd:PRK00064 234 DLLEALAKNRERDRARGRTLVGPHRDDLRFRING-LPAADFGSTGQQKLLLLALKLAEAELLKEETGEAPILLLDDVASE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502141139 319 LDDKRRQYLIEFLIGLNMQLWVTTTNLEGIENFATKAQLIKL 360
Cdd:PRK00064 313 LDDGRRAALLERLKGLGAQVFITTTDLEDLADLLENAKIFHV 354
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
5-356 |
3.08e-102 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 305.16 E-value: 3.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLA 84
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVRAEVERDGREV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 85 EFTTQFKRSSNRRITeYNESKIANN-ELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMHE 163
Cdd:COG1195 81 RLGLGLSRGGKKRVR-INGKPVRRLsDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLFQLDPRYLDALSRYERALKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 164 RNKILvEDIR--DDNWLKIIEEKMADISNHIANNRLKTLEFMQQAIDDLENEFPKADLSIDGIVEQKILNGKKNIVSFIT 241
Cdd:COG1195 160 RNALL-KQGReaDLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAALSGGKEELELRYRSGWLYESAELEEALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 242 AELYQTRSKDKLLGRTSFGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVHLDD 321
Cdd:COG1195 239 EALAENRERDLARGRTLVGPHRDDLEFTLNGKPA-KKFASQGQQKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDE 317
|
330 340 350
....*....|....*....|....*....|....*
gi 502141139 322 KRRQYLIEFLIGLNMQLWVTTTNLEGIENFATKAQ 356
Cdd:COG1195 318 ERREALLELLADLGGQVFITTTDPEDFPALLERAK 352
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
6-358 |
4.22e-50 |
|
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: 168.63 E-value: 4.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 6 LHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSKLGLAE 85
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISAVLERQGGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 86 FTTQFKRSSNRRIteynesKIANNELSKFTSM------VWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEY 159
Cdd:cd03242 81 LELTIRSGGGRKA------RLNGIKVRRLSDLlgvlnaVWFAPEDLELVKGSPADRRRFLDRLLGQLEPAYAHVLSEYQK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 160 YMHERNKILVedirddnwlkiieekmadisnhiannrlktlefmqqaiddlenefpkadlsidgiveqkilngkknivsf 239
Cdd:cd03242 155 ALRQRNALLK---------------------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 240 itaelyqtrskdkllgrtsfGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVHL 319
Cdd:cd03242 165 --------------------GPHRDDLLFFLNDKPA-ADFGSQGQQRTLALALKLAEIQLIKEVSGEYPVLLLDDVLAEL 223
|
330 340 350
....*....|....*....|....*....|....*....
gi 502141139 320 DDKRRQYLIEFLIGLnMQLWVTTTNLEGIENFATKAQLI 358
Cdd:cd03242 224 DLGRQAALLDAIEGR-VQTFVTTTDLADFDALWLRRAQI 261
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
5-348 |
7.79e-43 |
|
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: 152.51 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHCLVKALLQSK---- 80
Cdd:TIGR00611 2 YLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVIEGRVSKGdrev 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 81 -------LGLAEFTTQFKRSSNRRITEYNESkiannelskfTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAEL 153
Cdd:TIGR00611 82 tipleglLKKKGKKAKVNIDGQDKLSDLAGL----------LPMQLFAPEDLTLVKGSPKYRRRFLDWGLFQVEPVYLSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 154 VSKYEYYMHERNKILVEDIR---DDNWLKIIEEKMADISNHIANNRlktlefmQQAIDDLENEFPKAdlsidgivEQKIL 230
Cdd:TIGR00611 152 WSDYQRVLKQRNAALKQAQRqygDRTTLEVWDSQLAELGAKVSAWR-------AEFIEKLEPEAQKA--------HQLLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 231 NGKKNIVSF-----------ITAELYQTRSKDKLLGRTSFGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNY 299
Cdd:TIGR00611 217 PELESLSLFyrgelwdketdYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPV-EDFASQGQLRSLALALRLAEGEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502141139 300 AIKLTKIAPILLLDEVFVHLDDKRRQYLIEFLIGLNMQLWVTTTNLEGI 348
Cdd:TIGR00611 296 LREEGGEYPILLLDDVASELDDQRRRLLAELLQSLGVQVFVTAISLDHL 344
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
6-330 |
2.59e-25 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 104.87 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 6 LHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRgLRSAKLANVCKTSEDHCLVKALLQSKLGLAe 85
Cdd:PRK14079 3 LLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTGE-LPNGRLADLVRFGEGEAWVHAEVETGGGLS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 86 fTTQFKRSSNRRITEYNESKIANNELSKFTSMVWLTPH-MEGIFTSgSSDRRKFLDRIVYNFDPKHAELVSKYEYYMHER 164
Cdd:PRK14079 81 -RLEVGLGPGRRELKLDGVRVSLRELARLPGAVLIRPEdLELVLGP-PEGRRAYLDRLLSRLSARYAALLSAYERAVQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 165 NKILveDIRDDNWLKIIEEKMADISNHIANNRLKTL----EFMQQAIDDLENEFPkadLSIdGIVEQKILNGkknivsfI 240
Cdd:PRK14079 159 NAAL--KSGGGWGLHVWDDELVKLGDEIMALRRRALtrlsELAREAYAELGSRKP---LRL-ELSESTAPEG-------Y 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 241 TAELYQTRSKDKLLGRTSFGVHKSDFLVKHQKKNIlAKFCSTGEQKAILIAIILAEMNYAIKLTKIAPILLLDEVFVHLD 320
Cdd:PRK14079 226 LAALEARRAEELARGATVVGPHRDDLVLTLEGRPA-HRYASRGEARTVALALRLAEHRLLWEHFGEAPVLLVDDFTAELD 304
|
330
....*....|
gi 502141139 321 DKRRQYLIEF 330
Cdd:PRK14079 305 PRRRGALLAL 314
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-49 |
8.72e-11 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 61.94 E-value: 8.72e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 502141139 4 IFLHSLSLENYRNFKNLELKTDNTP--IILIGENGSGKTNILEAISLF 49
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPrlTVLVGENGSGKTTLLEAIALA 48
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
5-56 |
1.86e-10 |
|
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: 61.56 E-value: 1.86e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLFYPGRGLR 56
Cdd:COG3593 2 KLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
6-49 |
6.06e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.86 E-value: 6.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502141139 6 LHSLSLENYRNFKNLELKTDntPI-ILIGENGSGKTNILEAISLF 49
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLG--PLtVLIGANGSGKSNLLDALRFL 44
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
5-352 |
7.67e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 50.43 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 5 FLHSLSLENYRNFKN---LELKTDNTPI----ILIGENGSGKTNILEAISLfypgrglrsaklanvcktsedhcLVKALL 77
Cdd:COG1106 1 MLISFSIENFRSFKDeltLSMVASGLRLlrvnLIYGANASGKSNLLEALYF-----------------------LRNLVL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 78 QSKLGLAEFTTQFKRSSNRRiteyneskianNELSKFTSMVWLtphmegiftsgssDRRKFLDRIVYNFDPKHAELVsky 157
Cdd:COG1106 58 NSSQPGDKLVEPFLLDSESK-----------NEPSEFEILFLL-------------DGVRYEYGFELDKERIISEWL--- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 158 eYYMHERNKILVEDIRDD-NWLK---IIEEKMADISNHIANNrlktlEFMQQAIDDLENEfpkADLSIDGIVeqkilngk 233
Cdd:COG1106 111 -YFLSTAAQLNVPLLSPLyDWFDnniSLDTSSDGLTLLLKED-----ESLKEELLELLKI---ADPGIEDIE-------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 234 knivsfitaelYQTRSKDKLLGRTSFGVHksdflvKHQKKNILAKFCSTGEQKAILIAIILAEMNYAIKltkiapILLLD 313
Cdd:COG1106 174 -----------VEEEEIEDLVERKLIFKH------KGGNVPLPLSEESDGTKRLLALAGALLDALAKGG------VLLID 230
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502141139 314 EVFVHLDDKRRQYLIEFLIGL----NMQLWVTTTNLEGIENFA 352
Cdd:COG1106 231 EIEASLHPSLLRKLLKLFLDLanknNAQLIFTTHSTELLDAFL 273
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-342 |
1.33e-06 |
|
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: 49.31 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 30 ILIGENGSGKTNILEAISLFYPGRGLRSAKLANVCKTSEDHclvkallqsKLGLAEFTTQFKRSSNRRITEYNESKIANN 109
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIG---------GIPSLLNGIDPKEPIEFEISEFLEDGVRYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 110 ---ELSKFTSMVWLTPHMEGIFTSGSSDRRKFLDRIVYNFDPKHAELVSKYEYYMHERNKILVEDIRDDNWLKIIEEKma 186
Cdd:pfam13304 74 yglDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 187 DISNHIANNRLKTLEFMQQAIDDLENEFPKADLsidgivEQKILNGKKNIVSFITAELYqtRSKDKLLGRTSFGVHKSDF 266
Cdd:pfam13304 152 SFLLLLDEGLLLEDWAVLDLAADLALFPDLKEL------LQRLVRGLKLADLNLSDLGE--GIEKSLLVDDRLRERGLIL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502141139 267 LVKHQKKNILAKFCSTGEQKAILIAIILAEMNyaikltKIAPILLLDEVFVHLDDKRRQYLIEFL---IGLNMQLWVTT 342
Cdd:pfam13304 224 LENGGGGELPAFELSDGTKRLLALLAALLSAL------PKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTT 296
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-74 |
6.35e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 6.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502141139 6 LHSLSLENYRNFKNLELKTDNTPIILI-GENGSGKTNILEAISL-FYpGRGLRSAKL-ANVCKTSEDHCLVK 74
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDFDDGLNLIvGPNGAGKSTILEAIRYaLY-GKARSRSKLrSDLINVGSEEASVE 72
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
5-49 |
1.77e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 46.44 E-value: 1.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502141139 5 FLHSLSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISLF 49
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
6-50 |
2.70e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 2.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502141139 6 LHSLSLENYRNFKNLELKTDNTpIILIGENGSGKTNILEAISLFY 50
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKPL-TLLIGPNGSGKSTLIQALLLLL 44
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
15-46 |
4.38e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 41.29 E-value: 4.38e-04
10 20 30
....*....|....*....|....*....|..
gi 502141139 15 RNFKNLELKTDNTpiILIGENGSGKTNILEAI 46
Cdd:COG3910 28 RNLEGLEFHPPVT--FFVGENGSGKSTLLEAI 57
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
280-331 |
4.77e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.76 E-value: 4.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 502141139 280 CSTGEqKAILIAIIL-AEMNYAIKLTKIAP----ILLLDEVFVHLDDKRRQYLIEFL 331
Cdd:pfam13558 33 LSGGE-KQLLAYLPLaAALAAQYGSAEGRPpaprLVFLDEAFAKLDEENIRTALELL 88
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-48 |
6.49e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 6.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 502141139 9 LSLENYRNFKNLELKTDNTPIILIGENGSGKTNILEAISL 48
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKL 40
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
260-354 |
7.94e-04 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.54 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 260 GVHKSDFLVKHQKKNILAKF-CSTGEQKAILIAIILAEMnyaikltkiAPILLLDEVFVHLDDKRRQYLIEFLIGL---N 335
Cdd:cd00267 60 GKDIAKLPLEELRRRIGYVPqLSGGQRQRVALARALLLN---------PDLLLLDEPTSGLDPASRERLLELLRELaeeG 130
|
90
....*....|....*....
gi 502141139 336 MQLWVTTTNLEGIENFATK 354
Cdd:cd00267 131 RTVIIVTHDPELAELAADR 149
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-48 |
1.79e-03 |
|
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: 39.13 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 502141139 9 LSLENYRNFKNLELKTDNTPIILI-GENGSGKTNILEAISL 48
Cdd:cd03240 4 LSIRNIRSFHERSEIEFFSPLTLIvGQNGAGKTTIIEALKY 44
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
6-101 |
2.94e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 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: 213242 [Multi-domain] Cd Length: 247 Bit Score: 38.71 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502141139 6 LHSLSLENYRNFKNlelktdnTPII--------LIGENGSGKTNILEAISlFYPG---RGLRSAKL------ANVCKTSE 68
Cdd:cd03275 1 LKRLELENFKSYKG-------RHVIgpfdrftcIIGPNGSGKSNLMDAIS-FVLGeksSHLRSKNLkdliyrARVGKPDS 72
|
90 100 110
....*....|....*....|....*....|...
gi 502141139 69 DHCLVKALLQSKlglAEFTTQFKRSSNRRITEY 101
Cdd:cd03275 73 NSAYVTAVYEDD---DGEEKTFRRIITGGSSSY 102
|
|
| |
