|
Name |
Accession |
Description |
Interval |
E-value |
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-556 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 622.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSET--CAKQL 78
Cdd:COG0497 1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDppLAAWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 79 KKYDIYMEEDNIVtVTRKIS-EGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDSilELK 157
Cdd:COG0497 81 EENGLDLDDGELI-LRREISaDGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLE--ELL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 158 EQIKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNALsY 237
Cdd:COG0497 158 EEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-S 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 238 ETAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKLKYG 317
Cdd:COG0497 237 GGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 318 NSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEFEIQ 397
Cdd:COG0497 317 VTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 398 ITRKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKM 477
Cdd:COG0497 397 VTPLEEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741054027 478 AKISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHATEMKDMADR 556
Cdd:COG0497 477 ARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLALAAS 555
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
1-552 |
1.39e-140 |
|
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: 418.37 E-value: 1.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSV-SETCAKQLK 79
Cdd:TIGR00634 1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTeSLDDADYPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 80 KYDIYMEEDN---IVTVTRKIS-EGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDSilE 155
Cdd:TIGR00634 81 LQAIELEEEDedgEVILRRSISrDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGAN--E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 156 LKEQIKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNAL 235
Cdd:TIGR00634 159 KVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 236 SYE-TAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKL 314
Cdd:TIGR00634 239 RGDvDVQEGSLLEGLGEAQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 315 KYGNSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEF 394
Cdd:TIGR00634 319 KYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 395 EIQIT------RKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQ 468
Cdd:TIGR00634 399 TVEIKtslpsgAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 469 TAMKVAEKMAKISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHAT 548
Cdd:TIGR00634 479 TAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQ 558
|
....
gi 2741054027 549 EMKD 552
Cdd:TIGR00634 559 ELLE 562
|
|
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-550 |
7.26e-99 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 310.71 E-value: 7.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSETCAKQLKK 80
Cdd:PRK10869 1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 81 YDIYMEEDNIVTVTRKI-SEGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDsiLELKEQ 159
Cdd:PRK10869 81 EDNQLEDGNECLLRRVIsSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANE--TSLLQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 160 IKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNALSYET 239
Cdd:PRK10869 159 MRAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 240 AGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKLKYGNS 319
Cdd:PRK10869 239 EVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 320 IEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEFEIQIT 399
Cdd:PRK10869 319 PEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 400 -RKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKMA 478
Cdd:PRK10869 399 fDPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741054027 479 KISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHATEM 550
Cdd:PRK10869 479 QLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKEL 550
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
407-536 |
3.88e-62 |
|
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: 205.90 E-value: 3.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 407 NGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKMAKISRNHQV 486
Cdd:cd03241 147 GGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQV 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2741054027 487 ICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGG 536
Cdd:cd03241 227 LCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-186 |
3.56e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.43 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 5 LHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSETCAKQLKKY--D 82
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITfeN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 83 IYMEEDNIVTVTRKISE--GRSISKINGETVNIKTLKNVMSLLIdihGQHDHQSLLYTKNHLDILDKFAKDSILELKEQI 160
Cdd:pfam13476 81 NDGRYTYAIERSRELSKkkGKTKKKEILEILEIDELQQFISELL---KSDKIILPLLVFLGQEREEEFERKEKKERLEEL 157
|
170 180
....*....|....*....|....*.
gi 2741054027 161 KEEYSKYTKLIKKLEEFNIDEGQKAR 186
Cdd:pfam13476 158 EKALEEKEDEKKLLEKLLQLKEKKKE 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-556 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 622.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSET--CAKQL 78
Cdd:COG0497 1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDppLAAWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 79 KKYDIYMEEDNIVtVTRKIS-EGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDSilELK 157
Cdd:COG0497 81 EENGLDLDDGELI-LRREISaDGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLE--ELL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 158 EQIKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNALsY 237
Cdd:COG0497 158 EEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-S 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 238 ETAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKLKYG 317
Cdd:COG0497 237 GGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 318 NSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEFEIQ 397
Cdd:COG0497 317 VTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 398 ITRKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKM 477
Cdd:COG0497 397 VTPLEEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741054027 478 AKISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHATEMKDMADR 556
Cdd:COG0497 477 ARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLALAAS 555
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
1-552 |
1.39e-140 |
|
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: 418.37 E-value: 1.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSV-SETCAKQLK 79
Cdd:TIGR00634 1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTeSLDDADYPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 80 KYDIYMEEDN---IVTVTRKIS-EGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDSilE 155
Cdd:TIGR00634 81 LQAIELEEEDedgEVILRRSISrDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGAN--E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 156 LKEQIKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNAL 235
Cdd:TIGR00634 159 KVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 236 SYE-TAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKL 314
Cdd:TIGR00634 239 RGDvDVQEGSLLEGLGEAQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 315 KYGNSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEF 394
Cdd:TIGR00634 319 KYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 395 EIQIT------RKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQ 468
Cdd:TIGR00634 399 TVEIKtslpsgAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 469 TAMKVAEKMAKISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHAT 548
Cdd:TIGR00634 479 TAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQ 558
|
....
gi 2741054027 549 EMKD 552
Cdd:TIGR00634 559 ELLE 562
|
|
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-550 |
7.26e-99 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 310.71 E-value: 7.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 1 MLLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSETCAKQLKK 80
Cdd:PRK10869 1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 81 YDIYMEEDNIVTVTRKI-SEGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILDKFAKDsiLELKEQ 159
Cdd:PRK10869 81 EDNQLEDGNECLLRRVIsSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANE--TSLLQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 160 IKEEYSKYTKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKKLSNSKEIVSALSEIYNALSYET 239
Cdd:PRK10869 159 MRAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 240 AGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLDVINHLKLKYGNS 319
Cdd:PRK10869 239 EVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 320 IEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDLNFIAVEFEIQIT 399
Cdd:PRK10869 319 PEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 400 -RKESIGENGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKMA 478
Cdd:PRK10869 399 fDPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741054027 479 KISRNHQVICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGGSGITEAGLIHATEM 550
Cdd:PRK10869 479 QLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKEL 550
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
407-536 |
3.88e-62 |
|
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: 205.90 E-value: 3.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 407 NGFDNVEFMISTNPGESVKPLVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKMAKISRNHQV 486
Cdd:cd03241 147 GGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQV 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2741054027 487 ICISHLSQIAAMADSHYLIKKTADENSTTTSIKKLTRQQSIEELVRINGG 536
Cdd:cd03241 227 LCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
2-146 |
8.41e-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: 170.46 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 2 LLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSETCAKQLKKY 81
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741054027 82 DIYMEEDNIVTVTRKIS-EGRSISKINGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNHLDILD 146
Cdd:cd03241 81 ELGIEDDDDLIIRREISrKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLD 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-514 |
2.30e-12 |
|
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: 65.07 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 427 LVKVASGGELSRIMLAIKSILATEDDIDTLIFDEIDTGISGQTAMKVAEKMAKIS-RNHQVICISHLSQIAAMADSHYLI 505
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 2741054027 506 KKTADENST 514
Cdd:cd03227 154 KKVITGVYK 162
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-186 |
3.56e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.43 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 5 LHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASKDMIRKGTDYSLVELTFSVSETCAKQLKKY--D 82
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITfeN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 83 IYMEEDNIVTVTRKISE--GRSISKINGETVNIKTLKNVMSLLIdihGQHDHQSLLYTKNHLDILDKFAKDSILELKEQI 160
Cdd:pfam13476 81 NDGRYTYAIERSRELSKkkGKTKKKEILEILEIDELQQFISELL---KSDKIILPLLVFLGQEREEEFERKEKKERLEEL 157
|
170 180
....*....|....*....|....*.
gi 2741054027 161 KEEYSKYTKLIKKLEEFNIDEGQKAR 186
Cdd:pfam13476 158 EKALEEKEDEKKLLEKLLQLKEKKKE 183
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-70 |
1.20e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.10 E-value: 1.20e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2741054027 1 MLLNLHVKNL-ALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASK------DMIRKGTDYSLVELTFSV 70
Cdd:COG0419 1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSrsklrsDLINVGSEEASVELEFEH 77
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
432-505 |
6.16e-07 |
|
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: 49.17 E-value: 6.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2741054027 432 SGGELSRIMLAikSILATEDDIdtLIFDEIDTGISGQTAMKVAEKMAKIS-RNHQVICISHLSQIAAMADSHYLI 505
Cdd:cd00267 82 SGGQRQRVALA--RALLLNPDL--LLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAADRVIV 152
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
65-510 |
3.42e-06 |
|
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: 49.97 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 65 ELTFSVSETCAKQLKKYDIYMEEDNIVTVTRKISEGRSISK---INGETVNIKTLKNVMSLLIDIHGQHDHQSLLYTKNH 141
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKqkiDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 142 LDILDKFAKDSILELKEQIKEEYSKYTKLIKKLEEFNID----EGQKAREIEFAEYEVNEIESANLKPEEDVQVEEEFKK 217
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEqlliEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 218 LSNSKEIVSALSEIynaLSYETAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTSQIYDYNsgMDFNPE 297
Cdd:pfam02463 862 EITKEELLQELLLK---EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL--LKYEEE 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 298 YVRKVEERLDVINHLKLKYGNSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELE 377
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 378 VLVKQALVDLNFIAVEFEIQITRKES--IGENGFDNVEFMISTN-------PGESVKPLvKVASGGELSRIMLAIksILA 448
Cdd:pfam02463 1017 QRLKEFLELFVSINKGWNKVFFYLELggSAELRLEDPDDPFSGGieisarpPGKGVKNL-DLLSGGEKTLVALAL--IFA 1093
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741054027 449 TE--DDIDTLIFDEIDTGISGQTAMKVAEKMAKISRNHQVICISHLSQIAAMADSHYLIKKTAD 510
Cdd:pfam02463 1094 IQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVEN 1157
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
2-112 |
1.03e-05 |
|
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: 47.29 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 2 LLNLHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNK-----ASKDMIRKGTDYSLVELTFSVSetcak 76
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKshrtsRDKELIRWGAEEAKISAVLERQ----- 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 2741054027 77 qlkkydiYMEEDNIVTVTrkiSEGRSISKINGETVN 112
Cdd:cd03242 76 -------GGELALELTIR---SGGGRKARLNGIKVR 101
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
5-377 |
1.31e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 5 LHVKNLALIEEVDVDFEKGLIVLTGETGAGKSLILGSVNIAL-GNKASK---DMIRKGTDYSLVEL-------TFSVSET 73
Cdd:PRK01156 6 IRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALfTDKRTEkieDMIKKGKNNLEVELefrigghVYQIRRS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 74 CAKQLK--KYDIYMEEDNIVtVTRKISEGRSISKINGETVNIKTLKNVMSLlidihGQHDHQSLLY--TKNHLDILDKfa 149
Cdd:PRK01156 86 IERRGKgsRREAYIKKDGSI-IAEGFDDTTKYIEKNILGISKDVFLNSIFV-----GQGEMDSLISgdPAQRKKILDE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 150 kdsILELkEQIKEEYSKYTKLIKKLEEfnidegqkarEIEFAEYEVNEIESANLKPEE-DVQVEEEFKKLSNSKEIVSAL 228
Cdd:PRK01156 158 ---ILEI-NSLERNYDKLKDVIDMLRA----------EISNIDYLEEKLKSSNLELENiKKQIADDEKSHSITLKEIERL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 229 SEIYNALSYE---------TAGGLGDIINKAVMDINSIKGMDEKISQFQTELYDIDNLCRELTS-QIYDYNSGMDFNPEY 298
Cdd:PRK01156 224 SIEYNNAMDDynnlksalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdPVYKNRNYINDYFKY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 299 VRKVEERLDVINHLKLKYgNSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLS--EQRKKAAKEL 376
Cdd:PRK01156 304 KNDIENKKQILSNIDAEI-NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKsiESLKKKIEEY 382
|
.
gi 2741054027 377 E 377
Cdd:PRK01156 383 S 383
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-72 |
7.43e-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: 44.14 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 2 LLNLHVKNLALIEEV-DVDFEKGLIVLTGETGAGKSLILGSVNIAL---------GNKASKDMIRKGTDYSLVELTFSVS 71
Cdd:cd03240 1 IDKLSIRNIRSFHERsEIEFFSPLTLIVGQNGAGKTTIIEALKYALtgelppnskGGAHDPKLIREGEVRAQVKLAFENA 80
|
.
gi 2741054027 72 E 72
Cdd:cd03240 81 N 81
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
18-69 |
1.62e-04 |
|
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: 42.97 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 18 VDFEKGLIVLTGETGAGKSLILGSVNIALGNKAS--------KDMIRKGTDYSLVELTFS 69
Cdd:cd03276 17 IEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASdtnrgsslKDLIKDGESSAKITVTLK 76
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
6-112 |
1.74e-04 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 43.99 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 6 HVKNLAL-----IEEVDVDFEKGLIVLTGETGAGKSLILGSVNI-ALG----NKASKDMIRKGTDYSLVELTFSvsetca 75
Cdd:PRK00064 2 YLTRLSLtdfrnYEELDLELSPGVNVLVGENGQGKTNLLEAIYLlAPGrshrTARDKELIRFGAEAAVIHGRVE------ 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 2741054027 76 kqlkkydiyMEEDNIVTVTRKISEGRSISKINGETVN 112
Cdd:PRK00064 76 ---------KGGRELPLGLEIDKKGGRKVRINGEPQR 103
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-83 |
1.28e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 3 LNLHVKNL-ALIEEVDVDFEK----GLIVLTGETGAGKSLILGSVNIALGNKASK--DMIRKGTDYSLVELTFSVSETCA 75
Cdd:cd03279 4 LKLELKNFgPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALYGKTPRygRQENLRSVFAPGEDTAEVSFTFQ 83
|
....*...
gi 2741054027 76 KQLKKYDI 83
Cdd:cd03279 84 LGGKKYRV 91
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
14-397 |
1.51e-03 |
|
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: 41.50 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 14 EEVDVDFEKGLIVLTGETGAGKSLILGSVNIALGNKASK--------DMI----RKGTDYSLVELTFSVSETcakqlkky 81
Cdd:pfam02463 15 KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKslrserlsDLIhsksGAFVNSAEVEITFDNEDH-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 82 DIYMEEDNIVTVTRKISEGRSISKINGETVNIKTLKNVM-SLLIDIHGQH-------DHQSLLYTKNHLDILDKFAkdSI 153
Cdd:pfam02463 87 ELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLeSQGISPEAYNflvqggkIEIIAMMKPERRLEIEEEA--AG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 154 LELKEQIKEEYSKY-TKLIKKLEEFNIDEGQKAREIEFAEYEVNEIESANLKPEEDVQVEEE--FKKLSNSKEIVSALSE 230
Cdd:pfam02463 165 SRLKRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyLDYLKLNEERIDLLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 231 IYNALSYETAGGLGDIINKAVM--DINSIKGMDEKISQFQTELYD-IDNLCRELTSQIYDYNSGMDFNPEYVRKVEERLD 307
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 308 VINHLKLKYGNSIEEILRYKEEKEEYLEKLNNMTDEMESVKNQISELEGTLNNLCTKLSEQRKKAAKELEVLVKQALVDL 387
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
410
....*....|
gi 2741054027 388 NFIAVEFEIQ 397
Cdd:pfam02463 405 KEAQLLLELA 414
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
383-513 |
1.67e-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: 39.90 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741054027 383 ALVDLNFIAVE-FEIQITRKESIgengFDNVEFmisTNPGESVKPLV---KVASGGELSRIMLAIKSILAT--EDDIDTL 456
Cdd:cd03240 71 AQVKLAFENANgKKYTITRSLAI----LENVIF---CHQGESNWPLLdmrGRCSGGEKVLASLIIRLALAEtfGSNCGIL 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741054027 457 IFDEIDTGISGQtamKVAEKMAKI------SRNHQVICISHLSQIAAMADSHYLIKKTADENS 513
Cdd:cd03240 144 ALDEPTTNLDEE---NIEESLAEIieerksQKNFQLIVITHDEELVDAADHIYRVEKDGRQKS 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
432-500 |
6.64e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 39.12 E-value: 6.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741054027 432 SGGELSRIMLAIksILATEDDIdtLIFDEIDTGISGQTAMKVAEKMAKISRNHQ--VICISH-LSQIAAMAD 500
Cdd:COG1123 144 SGGQRQRVAIAM--ALALDPDL--LIADEPTTALDVTTQAEILDLLRELQRERGttVLLITHdLGVVAEIAD 211
|
|
| |
