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Conserved domains on  [gi|1125492745|gb|OLE14568|]
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DNA repair protein RecN [Acidobacteria bacterium 13_1_20CM_4_56_7]

Protein Classification

DNA repair protein RecN( domain architecture ID 11423061)

DNA repair protein RecN may be involved in recombinational repair of damaged DNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-564 0e+00

DNA repair ATPase RecN [Replication, recombination and repair];


:

Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 654.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFR-PESAQINLIL 79
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDlSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 DEHGLESASEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAGIR--LDSL 155
Cdd:COG0497    81 EENGLDLDDGELILRREISAdgRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEelLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 156 AKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDLLYESSN 235
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 236 SVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDLLKRKYGNSVE 315
Cdd:COG0497   241 GALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 316 EIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-KARFHVEITTS 394
Cdd:COG0497   321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMpNARFEVEVTPL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 395 EDeanWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKaSVEAGHSRTngngkpkraasqRTLVFDEIDTGI 474
Cdd:COG0497   401 EE---PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALK-VVLADKDAV------------PTLIFDEVDTGV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 475 GGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSGAKLTDASLK 554
Cdd:COG0497   465 GGRVAEAVGEKLARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALA 544
                         570
                  ....*....|
gi 1125492745 555 HAEQMLKTNA 564
Cdd:COG0497   545 HARELLALAA 554
 
Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-564 0e+00

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 654.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFR-PESAQINLIL 79
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDlSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 DEHGLESASEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAGIR--LDSL 155
Cdd:COG0497    81 EENGLDLDDGELILRREISAdgRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEelLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 156 AKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDLLYESSN 235
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 236 SVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDLLKRKYGNSVE 315
Cdd:COG0497   241 GALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 316 EIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-KARFHVEITTS 394
Cdd:COG0497   321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMpNARFEVEVTPL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 395 EDeanWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKaSVEAGHSRTngngkpkraasqRTLVFDEIDTGI 474
Cdd:COG0497   401 EE---PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALK-VVLADKDAV------------PTLIFDEVDTGV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 475 GGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSGAKLTDASLK 554
Cdd:COG0497   465 GGRVAEAVGEKLARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALA 544
                         570
                  ....*....|
gi 1125492745 555 HAEQMLKTNA 564
Cdd:COG0497   545 HARELLALAA 554
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-562 1.91e-145

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: 431.08  E-value: 1.91e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFRPESAqinLILD 80
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESL---DDAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  81 EHGLESAS-------EELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAGI- 150
Cdd:TIGR00634  78 YPALQAIEleeededGEVILRRSISRdgRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGAn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 151 -RLDSLAKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDL 229
Cdd:TIGR00634 158 eKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 230 LYE----SSNSVLSTLRSAARHLEElaRYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDL 305
Cdd:TIGR00634 238 LRGdvdvQEGSLLEGLGEAQLALAS--VIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKR 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 306 LKRKYGNSVEEIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-K 384
Cdd:TIGR00634 316 LKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMeK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 385 ARFHVEITTSEDE---ANWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKASVeaghsrtngngkPKRAAS 461
Cdd:TIGR00634 396 AEFTVEIKTSLPSgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVL------------SSSAAV 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 462 QrTLVFDEIDTGIGGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIAR 541
Cdd:TIGR00634 464 T-TLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELAR 542
                         570       580
                  ....*....|....*....|.
gi 1125492745 542 MLSGAKLTDASLKHAEQMLKT 562
Cdd:TIGR00634 543 MLAGLEKSDLTLAHAQELLEA 563
PRK10869 PRK10869
recombination and repair protein; Provisional
1-560 4.83e-105

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 326.50  E-value: 4.83e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFRPESAQINL-IL 79
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALrWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 DEHGLESaSEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAG--IRLDSL 155
Cdd:PRK10869   81 EDNQLED-GNECLLRRVISSdgRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANetSLLQEM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 156 AKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDLLYESS- 234
Cdd:PRK10869  160 RAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEe 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 235 NSVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDLLKRKYGNSV 314
Cdd:PRK10869  240 VNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 315 EEIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-KARFHVEITT 393
Cdd:PRK10869  320 EELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMpHGKFTIDVKF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 394 seDEANWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKASVeaghsrtngngkpKRAASQRTLVFDEIDTG 473
Cdd:PRK10869  400 --DPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVIT-------------ARKMETPALIFDEVDVG 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 474 IGGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSGAKLTDASL 553
Cdd:PRK10869  465 ISGPTAAVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTL 544

                  ....*..
gi 1125492745 554 KHAEQML 560
Cdd:PRK10869  545 ANAKELL 551
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
403-545 2.36e-58

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: 195.88  E-value: 2.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 403 SGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKAsVEAGHSRTngngkpkraasqRTLVFDEIDTGIGGSAAEAV 482
Cdd:cd03241   147 GGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKA-ILARKDAV------------PTLIFDEIDTGISGEVAQAV 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125492745 483 GKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSG 545
Cdd:cd03241   214 GKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
AAA_23 pfam13476
AAA domain;
5-190 5.04e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 55.97  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   5 LRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKAS--PEVVRYGAEKAVVSCVFRPE-SAQINLIL-- 79
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlKRKSGGGFVKGDIRIGLEGKgKAYVEITFen 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 -DEHGLESASEELILKREIASKSRVWINNQPATVGvLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAgiRLDSLAKT 158
Cdd:pfam13476  81 nDGRYTYAIERSRELSKKKGKTKKKEILEILEIDE-LQQFISELLKSDKIILPLLVFLGQEREEEFERKE--KKERLEEL 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1125492745 159 HTAWRELRIRIDELERSEQDRLRLVDLWNFQK 190
Cdd:pfam13476 158 EKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
 
Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-564 0e+00

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 654.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFR-PESAQINLIL 79
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDlSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 DEHGLESASEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAGIR--LDSL 155
Cdd:COG0497    81 EENGLDLDDGELILRREISAdgRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEelLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 156 AKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDLLYESSN 235
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 236 SVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDLLKRKYGNSVE 315
Cdd:COG0497   241 GALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 316 EIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-KARFHVEITTS 394
Cdd:COG0497   321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMpNARFEVEVTPL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 395 EDeanWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKaSVEAGHSRTngngkpkraasqRTLVFDEIDTGI 474
Cdd:COG0497   401 EE---PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALK-VVLADKDAV------------PTLIFDEVDTGV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 475 GGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSGAKLTDASLK 554
Cdd:COG0497   465 GGRVAEAVGEKLARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALA 544
                         570
                  ....*....|
gi 1125492745 555 HAEQMLKTNA 564
Cdd:COG0497   545 HARELLALAA 554
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-562 1.91e-145

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: 431.08  E-value: 1.91e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFRPESAqinLILD 80
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESL---DDAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  81 EHGLESAS-------EELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAGI- 150
Cdd:TIGR00634  78 YPALQAIEleeededGEVILRRSISRdgRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGAn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 151 -RLDSLAKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDL 229
Cdd:TIGR00634 158 eKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 230 LYE----SSNSVLSTLRSAARHLEElaRYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDL 305
Cdd:TIGR00634 238 LRGdvdvQEGSLLEGLGEAQLALAS--VIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKR 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 306 LKRKYGNSVEEIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-K 384
Cdd:TIGR00634 316 LKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMeK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 385 ARFHVEITTSEDE---ANWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKASVeaghsrtngngkPKRAAS 461
Cdd:TIGR00634 396 AEFTVEIKTSLPSgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVL------------SSSAAV 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 462 QrTLVFDEIDTGIGGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIAR 541
Cdd:TIGR00634 464 T-TLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELAR 542
                         570       580
                  ....*....|....*....|.
gi 1125492745 542 MLSGAKLTDASLKHAEQMLKT 562
Cdd:TIGR00634 543 MLAGLEKSDLTLAHAQELLEA 563
PRK10869 PRK10869
recombination and repair protein; Provisional
1-560 4.83e-105

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 326.50  E-value: 4.83e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFRPESAQINL-IL 79
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALrWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 DEHGLESaSEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAG--IRLDSL 155
Cdd:PRK10869   81 EDNQLED-GNECLLRRVISSdgRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANetSLLQEM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 156 AKTHTAWRELRIRIDELERSEQDRLRLVDLWNFQKTEIDAAKLESGEDLRLESERRVLMNAEKLYTAAMSSYDLLYESS- 234
Cdd:PRK10869  160 RAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEe 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 235 NSVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARDYADGIDASPERLAEIEDRLASIDLLKRKYGNSV 314
Cdd:PRK10869  240 VNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 315 EEIIAFGIDLEQKLNDIENREEILRGLRKQLAAAAQAYLAEAQTVSRTRASAASKLEKLAESEINELAI-KARFHVEITT 393
Cdd:PRK10869  320 EELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMpHGKFTIDVKF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 394 seDEANWSPSGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKASVeaghsrtngngkpKRAASQRTLVFDEIDTG 473
Cdd:PRK10869  400 --DPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVIT-------------ARKMETPALIFDEVDVG 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 474 IGGSAAEAVGKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSGAKLTDASL 553
Cdd:PRK10869  465 ISGPTAAVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTL 544

                  ....*..
gi 1125492745 554 KHAEQML 560
Cdd:PRK10869  545 ANAKELL 551
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
403-545 2.36e-58

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: 195.88  E-value: 2.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 403 SGLDSVAYLISTNPGEPLSPIEKIASGGELSRVMLALKAsVEAGHSRTngngkpkraasqRTLVFDEIDTGIGGSAAEAV 482
Cdd:cd03241   147 GGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKA-ILARKDAV------------PTLIFDEIDTGISGEVAQAV 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125492745 483 GKKLKALGVHNQVLCVTHLPQIASFADHHLLIEKSESGGRTRTTIRQLDAKDRKAEIARMLSG 545
Cdd:cd03241   214 GKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-146 2.82e-44

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: 158.13  E-value: 2.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVF---RPESAQinLI 78
Cdd:cd03241     1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFdisDEEEAK--AL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  79 LDEHGLESaSEELILKREIAS--KSRVWINNQPATVGVLKQLAPELVTIHAQNETVMAFDPPARLKLIDS 146
Cdd:cd03241    79 LLELGIED-DDDLIIRREISRkgRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
AAA_23 pfam13476
AAA domain;
5-190 5.04e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 55.97  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   5 LRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKAS--PEVVRYGAEKAVVSCVFRPE-SAQINLIL-- 79
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlKRKSGGGFVKGDIRIGLEGKgKAYVEITFen 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  80 -DEHGLESASEELILKREIASKSRVWINNQPATVGvLKQLAPELVTIHAQNETVMAFDPPARLKLIDSFAgiRLDSLAKT 158
Cdd:pfam13476  81 nDGRYTYAIERSRELSKKKGKTKKKEILEILEIDE-LQQFISELLKSDKIILPLLVFLGQEREEEFERKE--KKERLEEL 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1125492745 159 HTAWRELRIRIDELERSEQDRLRLVDLWNFQK 190
Cdd:pfam13476 158 EKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-69 4.44e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 53.48  E-value: 4.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125492745   1 MLVELRVENYAVI-DQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKAS------PEVVRYGAEKAVVSCVFR 69
Cdd:COG0419     1 KLLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARsrsklrSDLINVGSEEASVELEFE 76
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
2-92 1.14e-07

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: 51.59  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAviDQVVVEFGPG-LNLLTGETGAGKSILIDALALLMGDKASPEVVRYGAEKAVVSCVFRPEsaqinLILD 80
Cdd:cd03227     2 IVLGRFPSYF--VPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAE-----LIFT 74
                          90
                  ....*....|..
gi 1125492745  81 EHGLESASEELI 92
Cdd:cd03227    75 RLQLSGGEKELS 86
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1-400 2.46e-07

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: 53.82  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745    1 MLVELRVEN---YAviDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKAS--------PEVVRYGAEKAVVSCvfr 69
Cdd:pfam02463    1 YLKRIEIEGfksYA--KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkslrserlSDLIHSKSGAFVNSA--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   70 peSAQINLILDEHGLESASEELILKREIASK--SRVWINNQPATVGVLKQLAPEL-VTIHAQN-------ETVMAFDPPA 139
Cdd:pfam02463   76 --EVEITFDNEDHELPIDKEEVSIRRRVYRGgdSEYYINGKNVTKKEVAELLESQgISPEAYNflvqggkIEIIAMMKPE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  140 RLKLIDSFAGI------RLDSLAKTHTAWRELRIRIDELERSEQDRLRLVdlWNFQKTEIDAAKLesgEDLRLESERRVL 213
Cdd:pfam02463  154 RRLEIEEEAAGsrlkrkKKEALKKLIEETENLAELIIDLEELKLQELKLK--EQAKKALEYYQLK---EKLELEEEYLLY 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  214 MNAEKLYTAAMSSY-DLLYESSNSVLSTLRSAARHLEELARYDPQFGESLKLIESARADIEDVSTTARdyadgidaspER 292
Cdd:pfam02463  229 LDYLKLNEERIDLLqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE----------EL 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  293 LAEIEDRLASIDLLKRKYGNSVEEIIAFGIDLEQKLNDIENREEILRGLRKQLAAAaqaylaeaqtvsRTRASAASKLEK 372
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE------------EEEEEELEKLQE 366
                          410       420
                   ....*....|....*....|....*...
gi 1125492745  373 LAESEINELAIKARFHVEITTSEDEANW 400
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKE 394
AAA_29 pfam13555
P-loop containing region of AAA domain;
2-49 8.08e-07

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 46.44  E-value: 8.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAVIDQVVVEFGP-GLNLLTGETGAGKSILIDAL-ALLMGDK 49
Cdd:pfam13555   1 LTRLQLINWGTFDGHTIPIDPrGNTLLTGPSGSGKSTLLDAIqTLLVPAK 50
PRK01156 PRK01156
chromosome segregation protein; Provisional
1-341 1.52e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.06  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   1 MLVE-LRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALAL-LMGDKAS---PEVVRYGAEKAVVSCVFRPESA-- 73
Cdd:PRK01156    1 MIIKrIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFaLFTDKRTekiEDMIKKGKNNLEVELEFRIGGHvy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  74 QINLILDEHGLESASEELILKR-EIASKSRVWINN--QPATVGVLKQLAPELVTI-HAQNETVMAFDPPARLKLIDSFAG 149
Cdd:PRK01156   81 QIRRSIERRGKGSRREAYIKKDgSIIAEGFDDTTKyiEKNILGISKDVFLNSIFVgQGEMDSLISGDPAQRKKILDEILE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 150 IrlDSLAKTHTAWRE----LRIRIDELERSEQD-RLRLVDLWNFQKTEIDAAKLESgeDLRLESERrvlmnAEKLYTAAM 224
Cdd:PRK01156  161 I--NSLERNYDKLKDvidmLRAEISNIDYLEEKlKSSNLELENIKKQIADDEKSHS--ITLKEIER-----LSIEYNNAM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 225 SSYDLLYESSNSVLSTLRSAARHLEELARydpqfgeslklIESARADIEDVSTTardyadgIDASPERLAEIEDRLASId 304
Cdd:PRK01156  232 DDYNNLKSALNELSSLEDMKNRYESEIKT-----------AESDLSMELEKNNY-------YKELEERHMKIINDPVYK- 292
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1125492745 305 llkrkygnSVEEIIAFGIDleqkLNDIENREEILRGL 341
Cdd:PRK01156  293 --------NRNYINDYFKY----KNDIENKKQILSNI 317
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-45 2.17e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 49.93  E-value: 2.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1125492745   1 MLVELRVENYAVIDQVVVEFGPgLNLLTGETGAGKSILIDALALL 45
Cdd:COG4637     1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFL 44
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
2-77 8.09e-06

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 47.21  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGdkASPEV----------VRYGAEKAVVSCVFRPE 71
Cdd:cd03277     3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLG--GKPKLlgrakkvgefVKRGCDEGTIEIELYGN 80

                  ....*.
gi 1125492745  72 SAQINL 77
Cdd:cd03277    81 PGNIQV 86
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
427-521 1.33e-05

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: 45.43  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 427 ASGGELSRVMLALKASVEAGHSRTngngkpkraasqrTLVFDEIDTGIGGSAAEAVGKKLKALGVH-NQVLCVTHLPQIA 505
Cdd:cd03227    78 LSGGEKELSALALILALASLKPRP-------------LYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELA 144
                          90
                  ....*....|....*.
gi 1125492745 506 SFADHHLLIEKSESGG 521
Cdd:cd03227   145 ELADKLIHIKKVITGV 160
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-91 1.36e-05

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: 47.30  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEVVR--------YGAEKAVVSCVFRpesA 73
Cdd:COG3593     3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEedfylgddPDLPEIEIELTFG---S 79
                          90
                  ....*....|....*...
gi 1125492745  74 QINLILDEHGLESASEEL 91
Cdd:COG3593    80 LLSRLLRLLLKEEDKEEL 97
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
9-121 1.95e-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: 46.52  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   9 NYAVIDqvvVEFGPGLNLLTGETGAGKSILIDA---LALLMGDKAS--PEVVRYGAekavvscvfrpESAQINLILDEHG 83
Cdd:cd03242    11 NYAELE---LEFEPGVTVLVGENAQGKTNLLEAislLATGKSHRTSrdKELIRWGA-----------EEAKISAVLERQG 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1125492745  84 LESAsEELILKREIASKSRVWINNQPAT---VGVLK--QLAPE 121
Cdd:cd03242    77 GELA-LELTIRSGGGRKARLNGIKVRRLsdlLGVLNavWFAPE 118
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
18-69 1.37e-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: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  18 VEFGPGLNLLTGETGAGKSILIDALALLMGDKAS--------PEVVRYGAEKAVVSCVFR 69
Cdd:cd03276    17 IEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASdtnrgsslKDLIKDGESSAKITVTLK 76
recF PRK00064
recombination protein F; Reviewed
2-121 1.72e-04

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 43.99  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   2 LVELRVENYAVIDQVVVEFGPGLNLLTGETGAGKSILIDALALLmgdkaSP----------EVVRYGAEKAVVscvfrpe 71
Cdd:PRK00064    3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLL-----APgrshrtardkELIRFGAEAAVI------- 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1125492745  72 SAQINLILDEHGLEsaseeliLKREIASKSRVWINNQPAT-----VGVLK--QLAPE 121
Cdd:PRK00064   71 HGRVEKGGRELPLG-------LEIDKKGGRKVRINGEPQRklaelAGLLNvvLFTPE 120
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
14-69 2.07e-04

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: 42.59  E-value: 2.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125492745  14 DQVVVEFGPGLNLLTGETGAGKSILIDALAL-LMGDKA--------SPEVVRYGAEKAVVSCVFR 69
Cdd:cd03240    14 ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYaLTGELPpnskggahDPKLIREGEVRAQVKLAFE 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-46 3.44e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1125492745    2 LVELRVENYAVIDQVV-VEFGPGLNLLTGETGAGKSILIDALALLM 46
Cdd:COG4913      3 LQRLQLINWGTFDGVHtIDFDGRGTLLTGDNGSGKSTLLDAIQTLL 48
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
16-343 3.78e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   16 VVVEFGPGLNLLTGETGAGKSILIDALALLMGDKASPEV-------------VRYGAEKAVVSCVFRpesaqinlilDEH 82
Cdd:TIGR02169   17 KVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMraerlsdlisngkNGQSGNEAYVTVTFK----------NDD 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745   83 GLESASEELILKREI---ASKSRVWINNQPATVG-VLKQLAPELVTIHAQNeTVMAFD--------PPARLKLIDSFAGI 150
Cdd:TIGR02169   87 GKFPDELEVVRRLKVtddGKYSYYYLNGQRVRLSeIHDFLAAAGIYPEGYN-VVLQGDvtdfismsPVERRKIIDEIAGV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  151 -RLDSlaKTHTAWRELririDELERSEqDRLRLV---DLWNFQKTEIDAAKLESGEDLRLESErrvlmnaEKLYTAAMSS 226
Cdd:TIGR02169  166 aEFDR--KKEKALEEL----EEVEENI-ERLDLIideKRQQLERLRREREKAERYQALLKEKR-------EYEGYELLKE 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745  227 YDLLYESSNSVLSTLRSAARHLEELARydpQFGESLKLIESARADIEDVSTTARDYADG-IDASPERLAEIEDRLA---- 301
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTE---EISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIAsler 308
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1125492745  302 SIDLLKRKYGNSVEEIIAFGIDLEQKLNDIENREEILRGLRK 343
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
COG4637 COG4637
Predicted ATPase [General function prediction only];
463-542 4.40e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 42.61  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125492745 463 RTLVFDEIDTGIGGSAAEAVGKKLKALGVHNQVLCVTHLPQIASF--ADHHLLIEKSESGGrtrTTIRQLDAKDRKAEIA 540
Cdd:COG4637   280 PLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDAlePEEVLVLEREDDGE---TRIRRLSDLELPEWLE 356

                  ..
gi 1125492745 541 RM 542
Cdd:COG4637   357 GY 358
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
1-45 3.05e-03

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 40.03  E-value: 3.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1125492745   1 MLVELRVENYAVI-DQVVVEFGPG------LNLLTGETGAGKSILIDALALL 45
Cdd:COG1106     1 MLISFSIENFRSFkDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFL 52
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
3-69 8.22e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 38.02  E-value: 8.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125492745   3 VELRVENYAVIDQVVVEFGPG-LNLLTGETGAGKSILIDALALLMGDKASPEVVR-----YGAEKAVVSCVFR 69
Cdd:COG2401    36 VELRVVERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDvpdnqFGREASLIDAIGR 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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