|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-460 |
0e+00 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 571.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:PRK10869 4 QLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWLEDN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSdnpNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:PRK10869 84 QLEDG---NECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDND-L 239
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEeV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNE 319
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 320 TLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHN 399
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 400 LEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEV 461
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-460 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 549.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:COG0497 4 ELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWLEEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSDNpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:COG0497 84 GLDLDDG--ELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDNDLN 240
Cdd:COG0497 162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 241 IDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNET 320
Cdd:COG0497 242 ALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 321 LWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHnL 400
Cdd:COG0497 322 LLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP-L 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 401 EKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:COG0497 401 EEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEV 460
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
2-460 |
6.42e-139 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 410.28 E-value: 6.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQT-DSPAFLWLKEH 80
Cdd:TIGR00634 5 LRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESlDDADYPALQAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:TIGR00634 85 ELEEEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKVKAYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALS-DNDL 239
Cdd:TIGR00634 165 ELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRgDVDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVE-MDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITN 318
Cdd:TIGR00634 245 QEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKYGASV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 319 ETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDI-- 396
Cdd:TIGR00634 325 EEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTVEIkt 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572168737 397 ---QHNLEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:TIGR00634 405 slpSGAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEV 471
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1-151 |
3.89e-49 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 168.92 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:cd03241 3 ELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLLEL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 81 ELLDSDnpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAD 151
Cdd:cd03241 83 GIEDDD---DLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDGGLD 150
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-193 |
7.09e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 58.28 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLwlkEHE 81
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYV---EIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 82 LLDSDNPNECILRRMITI---EGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAdlhsLLDE 158
Cdd:pfam13476 78 FENNDGRYTYAIERSRELskkKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKE----KKER 153
|
170 180 190
....*....|....*....|....*....|....*
gi 572168737 159 MAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQ 193
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-460 |
0e+00 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 571.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:PRK10869 4 QLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWLEDN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSdnpNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:PRK10869 84 QLEDG---NECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDND-L 239
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEeV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNE 319
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 320 TLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHN 399
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 400 LEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEV 461
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-460 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 549.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:COG0497 4 ELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWLEEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSDNpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:COG0497 84 GLDLDDG--ELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDNDLN 240
Cdd:COG0497 162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 241 IDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNET 320
Cdd:COG0497 242 ALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 321 LWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHnL 400
Cdd:COG0497 322 LLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP-L 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 401 EKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:COG0497 401 EEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEV 460
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
2-460 |
6.42e-139 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 410.28 E-value: 6.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQT-DSPAFLWLKEH 80
Cdd:TIGR00634 5 LRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESlDDADYPALQAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 81 ELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:TIGR00634 85 ELEEEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKVKAYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALS-DNDL 239
Cdd:TIGR00634 165 ELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRgDVDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVE-MDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITN 318
Cdd:TIGR00634 245 QEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKYGASV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 319 ETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDI-- 396
Cdd:TIGR00634 325 EEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTVEIkt 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572168737 397 ---QHNLEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:TIGR00634 405 slpSGAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEV 471
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1-151 |
3.89e-49 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 168.92 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:cd03241 3 ELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLLEL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 81 ELLDSDnpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAD 151
Cdd:cd03241 83 GIEDDD---DLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDGGLD 150
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
390-460 |
4.01e-16 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 78.40 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 390 GEFFIDI--QH-NLEKLSP--------SGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFD 458
Cdd:cd03241 120 GSLLVDIhgQHdHQNLLNPerqldlldGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFD 199
|
..
gi 572168737 459 EV 460
Cdd:cd03241 200 EI 201
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-193 |
7.09e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 58.28 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLwlkEHE 81
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYV---EIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 82 LLDSDNPNECILRRMITI---EGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAdlhsLLDE 158
Cdd:pfam13476 78 FENNDGRYTYAIERSRELskkKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKE----KKER 153
|
170 180 190
....*....|....*....|....*....|....*
gi 572168737 159 MAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQ 193
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-388 |
7.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 150 ADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEfAIKEGEfEQLEEDQARLANAEQLLDVSQS 229
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-ELAELE-EELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 230 VMGALSDNDLNIDTMLYRAIRDLEELVEmdshysSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQ 309
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEE------ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572168737 310 LARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAME 388
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-333 |
4.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 106 FVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEA 185
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 186 RKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDndlnidtmlyraIRDLEELVEMDSHYSSA 265
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELEEELEELEEE 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572168737 266 LDMLNEALIQIQEASSEISQLAGNIEQD---PALLDELDNRISKTIQLARKHHITN---ETLWQHHQKLQQELQ 333
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDgelAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREERL 514
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
11-68 |
8.57e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 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: 213243 [Multi-domain] Cd Length: 198 Bit Score: 43.36 E-value: 8.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572168737 11 RHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYR--------SESSMIRNGVDKADITATFSMQ 68
Cdd:cd03276 13 RHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKasdtnrgsSLKDLIKDGESSAKITVTLKNQ 78
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-413 |
2.63e-04 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 151 DLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEfaIKEGEFEQLEEDQARLANAEQ-LLDVSQS 229
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAeIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 230 VMGALSDNDLNIdtmlyRAIRDLE-ELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTI 308
Cdd:TIGR02168 791 IEQLKEELKALR-----EALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 309 QLARKHHITNEtlwqHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRceagqklaeqvTQQIKQLAME 388
Cdd:TIGR02168 866 ELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-----------REKLAQLELR 930
|
250 260
....*....|....*....|....*
gi 572168737 389 NGEFFIDIQHNLEKLSPSGADVVEF 413
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-386 |
3.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 181 QENEARKQLLQYQVEELDEfaikegEFEQLEEDQARLANAEQLLDVSQSVMGALSDndlnidtmLYRAIRDLEELVEmds 260
Cdd:COG4913 606 FDNRAKLAALEAELAELEE------ELAEAEERLEALEAELDALQERREALQRLAE--------YSWDEIDVASAER--- 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 261 hyssALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHitnetlwQHHQKLQQELQTLLDFED 340
Cdd:COG4913 669 ----EIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-------KELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572168737 341 DEEQLIAEEQQAHqkciqLAEQIYQ-KRCEAGQKLAEQVTQQIKQLA 386
Cdd:COG4913 738 AAEDLARLELRAL-----LEERFAAaLGDAVERELRENLEERIDALR 779
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-389 |
5.13e-04 |
|
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: 42.65 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHF-AIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRN------------GVDKADITATFSm 67
Cdd:pfam02463 4 RIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSErlsdlihsksgaFVNSAEVEITFD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 68 qtDSPAFLWLKEHELldsdnpnecILRRMITIEGRSKAFVNNHPLPISQLRE-LGQYLIHLNGQHAPQLLLKSEyqlELV 146
Cdd:pfam02463 83 --NEDHELPIDKEEV---------SIRRRVYRGGDSEYYINGKNVTKKEVAElLESQGISPEAYNFLVQGGKIE---IIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 147 NNYADLHSLLDEMAEQYQIWRKLHKQVKNFRQ---QCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQL 223
Cdd:pfam02463 149 MMKPERRLEIEEEAAGSRLKRKKKEALKKLIEeteNLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 224 LDVSQSVMGALSDNDLNIDTMLYR--AIRDLEELVEMDSHYSSALDMLNEALIQIQEasSEISQLAGNIEQDPALLDELD 301
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQE--EELKLLAKEEEELKSELLKLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 302 NRISKTIQLARKHHITNETLWQHHQKLQQ---ELQTLLDFEDD----EEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKL 374
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEeieELEKELKELEIkreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
410
....*....|....*
gi 572168737 375 AEQVTQQIKQLAMEN 389
Cdd:pfam02463 387 SSAAKLKEEELELKS 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-388 |
5.34e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 155 LLDEMAEQYqiwRKLHKQV------KNFRQQCQENEARKQLLQYQV--EELDEFAIKEGEFE-QLEEDQARLANAEQLLD 225
Cdd:COG1196 194 ILGELERQL---EPLERQAekaeryRELKEELKELEAELLLLKLREleAELEELEAELEELEaELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 226 VSQSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHyssALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRIs 305
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEEL- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 306 ktiqlarkhhitnETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIyQKRCEAGQKLAEQVTQQIKQL 385
Cdd:COG1196 347 -------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEAL 412
|
...
gi 572168737 386 AME 388
Cdd:COG1196 413 LER 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-388 |
1.25e-03 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 14 VLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESS--------MIRNG------VDKADITATFSmqtdspaflwlKE 79
Cdd:TIGR02168 18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKAlrggkmedVIFNGsetrkpLSLAEVELVFD-----------NS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 80 HELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLREL--------------GQYLIHLNGQHAPQLLL-------- 137
Cdd:TIGR02168 87 DGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLfldtglgkrsysiiEQGKISEIIEAKPEERRaifeeaag 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 138 ---------KSEYQLELVN-NYADLHSLLDEMAEQyqiWRKLHKQVK---NFRQ-QCQENEARKQLLQYQVEELDE---- 199
Cdd:TIGR02168 167 iskykerrkETERKLERTReNLDRLEDILNELERQ---LKSLERQAEkaeRYKElKAELRELELALLVLRLEELREelee 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 200 --FAIKEGEfEQLEEDQARLANAEQLLDVSQSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQ 277
Cdd:TIGR02168 244 lqEELKEAE-EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 278 EASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCI 357
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
410 420 430
....*....|....*....|....*....|.
gi 572168737 358 QLAEqiyqKRCEAGQKLAEQVTQQIKQLAME 388
Cdd:TIGR02168 403 ERLE----ARLERLEDRRERLQQEIEELLKK 429
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-352 |
1.92e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 150 ADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEEL-DEFAIKEGEFEQLEEDQARL-ANAEQLLDVS 227
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeQELAALEAELAELEKEIAELrAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 228 QSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPA----LLDELDNR 303
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAeleaLLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572168737 304 ISKTIQLARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQA 352
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-66 |
2.06e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572168737 1 HLTINHF-AIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESS------MIRNGVDKADITATFS 66
Cdd:COG0419 4 RLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRsklrsdLINVGSEEASVELEFE 76
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-335 |
3.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 144 ELVNNYADL---HSLLDEMAEQyqiwRKLHKQVKNFRQQCQENEARKQLLQYQVEELD------EFAIKEGEFEQLEEDQ 214
Cdd:COG4913 229 ALVEHFDDLeraHEALEDAREQ----IELLEPIRELAERYAAARERLAELEYLRAALRlwfaqrRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 215 ARLANAEQLLDVSQ--------SVMGALSDNDLNIDTMLYRAIRDLEELVEmdsHYSSALDMLNEALIQIQ-EASSEISQ 285
Cdd:COG4913 305 ARLEAELERLEARLdalreeldELEAQIRGNGGDRLEQLEREIERLERELE---ERERRRARLEALLAALGlPLPASAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572168737 286 LAGNIEQDPALLDELDNRISKTIQLARKHHITNETLWQHHQKLQQELQTL 335
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1-68 |
4.85e-03 |
|
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: 37.72 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 1 HLTINHFAIVR-HLVLELNEG-MSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQ 68
Cdd:cd03227 1 KIVLGRFPSYFvPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAE 70
|
|
|