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Conserved domains on  [gi|572168737|gb|AHF50253|]
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recombination protein, partial [Vespertiliibacter genomosp. 1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10869 super family cl35963
recombination and repair protein; Provisional
1-460 0e+00

recombination and repair protein; Provisional


The actual alignment was detected with superfamily member PRK10869:

Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 571.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:PRK10869   4 QLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWLEDN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  81 ELLDSdnpNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:PRK10869  84 QLEDG---NECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDND-L 239
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEeV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNE 319
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 320 TLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHN 399
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 400 LEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEV 461
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-460 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 571.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:PRK10869   4 QLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWLEDN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  81 ELLDSdnpNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:PRK10869  84 QLEDG---NECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDND-L 239
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEeV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNE 319
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 320 TLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHN 399
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 400 LEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEV 461
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-460 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 549.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:COG0497    4 ELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWLEEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  81 ELLDSDNpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:COG0497   84 GLDLDDG--ELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEYR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDNDLN 240
Cdd:COG0497  162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEGG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 241 IDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNET 320
Cdd:COG0497  242 ALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 321 LWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHnL 400
Cdd:COG0497  322 LLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP-L 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 401 EKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:COG0497  401 EEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEV 460
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
2-460 6.42e-139

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 410.28  E-value: 6.42e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQT-DSPAFLWLKEH 80
Cdd:TIGR00634   5 LRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESlDDADYPALQAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   81 ELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:TIGR00634  85 ELEEEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKVKAYR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALS-DNDL 239
Cdd:TIGR00634 165 ELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRgDVDV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  240 NIDTMLYRAIRDLEELVE-MDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITN 318
Cdd:TIGR00634 245 QEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKYGASV 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  319 ETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDI-- 396
Cdd:TIGR00634 325 EEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTVEIkt 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572168737  397 ---QHNLEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:TIGR00634 405 slpSGAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEV 471
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
1-151 3.89e-49

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 168.92  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:cd03241    3 ELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLLEL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737  81 ELLDSDnpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAD 151
Cdd:cd03241   83 GIEDDD---DLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDGGLD 150
AAA_23 pfam13476
AAA domain;
2-193 7.09e-10

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 58.28  E-value: 7.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLwlkEHE 81
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYV---EIT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   82 LLDSDNPNECILRRMITI---EGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAdlhsLLDE 158
Cdd:pfam13476  78 FENNDGRYTYAIERSRELskkKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKE----KKER 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 572168737  159 MAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQ 193
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-460 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 571.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:PRK10869   4 QLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWLEDN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  81 ELLDSdnpNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:PRK10869  84 QLEDG---NECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDND-L 239
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEeV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 240 NIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNE 319
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 320 TLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHN 399
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737 400 LEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEV 461
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-460 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 549.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:COG0497    4 ELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWLEEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  81 ELLDSDNpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:COG0497   84 GLDLDDG--ELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEYR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDNDLN 240
Cdd:COG0497  162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGGEGG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 241 IDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNET 320
Cdd:COG0497  242 ALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 321 LWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDIQHnL 400
Cdd:COG0497  322 LLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP-L 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 401 EKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:COG0497  401 EEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEV 460
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
2-460 6.42e-139

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 410.28  E-value: 6.42e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQT-DSPAFLWLKEH 80
Cdd:TIGR00634   5 LRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESlDDADYPALQAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   81 ELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMA 160
Cdd:TIGR00634  85 ELEEEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKVKAYR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  161 EQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALS-DNDL 239
Cdd:TIGR00634 165 ELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRgDVDV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  240 NIDTMLYRAIRDLEELVE-MDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITN 318
Cdd:TIGR00634 245 QEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKYGASV 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  319 ETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAMENGEFFIDI-- 396
Cdd:TIGR00634 325 EEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTVEIkt 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572168737  397 ---QHNLEKLSPSGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFDEV 460
Cdd:TIGR00634 405 slpSGAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEV 471
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
1-151 3.89e-49

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 168.92  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLWLKEH 80
Cdd:cd03241    3 ELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLLEL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572168737  81 ELLDSDnpnECILRRMITIEGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAD 151
Cdd:cd03241   83 GIEDDD---DLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDGGLD 150
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
390-460 4.01e-16

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 78.40  E-value: 4.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 390 GEFFIDI--QH-NLEKLSP--------SGADVVEFNLRSNLGQQAQPLAKIASGGELSRISLAVQVLTANKLSTPTIIFD 458
Cdd:cd03241  120 GSLLVDIhgQHdHQNLLNPerqldlldGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFD 199

                 ..
gi 572168737 459 EV 460
Cdd:cd03241  200 EI 201
AAA_23 pfam13476
AAA domain;
2-193 7.09e-10

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 58.28  E-value: 7.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    2 LTINHFAIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQTDSPAFLwlkEHE 81
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYV---EIT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   82 LLDSDNPNECILRRMITI---EGRSKAFVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYAdlhsLLDE 158
Cdd:pfam13476  78 FENNDGRYTYAIERSRELskkKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKE----KKER 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 572168737  159 MAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQ 193
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-388 7.09e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 150 ADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEfAIKEGEfEQLEEDQARLANAEQLLDVSQS 229
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-ELAELE-EELEELEEELEELEEELEEAEE 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 230 VMGALSDNDLNIDTMLYRAIRDLEELVEmdshysSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQ 309
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEE------ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572168737 310 LARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKLAEQVTQQIKQLAME 388
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
106-333 4.03e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 106 FVNNHPLPISQLRELGQYLIHLNGQHAPQLLLKSEYQLELVNNYADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEA 185
Cdd:COG4717  293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 186 RKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQLLDVSQSVMGALSDndlnidtmlyraIRDLEELVEMDSHYSSA 265
Cdd:COG4717  373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELEEELEELEEE 440
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572168737 266 LDMLNEALIQIQEASSEISQLAGNIEQD---PALLDELDNRISKTIQLARKHHITN---ETLWQHHQKLQQELQ 333
Cdd:COG4717  441 LEELEEELEELREELAELEAELEQLEEDgelAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREERL 514
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
11-68 8.57e-05

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 43.36  E-value: 8.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572168737  11 RHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYR--------SESSMIRNGVDKADITATFSMQ 68
Cdd:cd03276   13 RHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKasdtnrgsSLKDLIKDGESSAKITVTLKNQ 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-413 2.63e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   151 DLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEELDEfaIKEGEFEQLEEDQARLANAEQ-LLDVSQS 229
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAeIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   230 VMGALSDNDLNIdtmlyRAIRDLE-ELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTI 308
Cdd:TIGR02168  791 IEQLKEELKALR-----EALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   309 QLARKHHITNEtlwqHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIYQKRceagqklaeqvTQQIKQLAME 388
Cdd:TIGR02168  866 ELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-----------REKLAQLELR 930
                          250       260
                   ....*....|....*....|....*
gi 572168737   389 NGEFFIDIQHNLEKLSPSGADVVEF 413
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTLEE 955
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-386 3.29e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  181 QENEARKQLLQYQVEELDEfaikegEFEQLEEDQARLANAEQLLDVSQSVMGALSDndlnidtmLYRAIRDLEELVEmds 260
Cdd:COG4913   606 FDNRAKLAALEAELAELEE------ELAEAEERLEALEAELDALQERREALQRLAE--------YSWDEIDVASAER--- 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  261 hyssALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHitnetlwQHHQKLQQELQTLLDFED 340
Cdd:COG4913   669 ----EIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-------KELEQAEEELDELQDRLE 737
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 572168737  341 DEEQLIAEEQQAHqkciqLAEQIYQ-KRCEAGQKLAEQVTQQIKQLA 386
Cdd:COG4913   738 AAEDLARLELRAL-----LEERFAAaLGDAVERELRENLEERIDALR 779
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1-389 5.13e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 5.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737     1 HLTINHF-AIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESSMIRN------------GVDKADITATFSm 67
Cdd:pfam02463    4 RIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSErlsdlihsksgaFVNSAEVEITFD- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    68 qtDSPAFLWLKEHELldsdnpnecILRRMITIEGRSKAFVNNHPLPISQLRE-LGQYLIHLNGQHAPQLLLKSEyqlELV 146
Cdd:pfam02463   83 --NEDHELPIDKEEV---------SIRRRVYRGGDSEYYINGKNVTKKEVAElLESQGISPEAYNFLVQGGKIE---IIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   147 NNYADLHSLLDEMAEQYQIWRKLHKQVKNFRQ---QCQENEARKQLLQYQVEELDEFAIKEGEFEQLEEDQARLANAEQL 223
Cdd:pfam02463  149 MMKPERRLEIEEEAAGSRLKRKKKEALKKLIEeteNLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   224 LDVSQSVMGALSDNDLNIDTMLYR--AIRDLEELVEMDSHYSSALDMLNEALIQIQEasSEISQLAGNIEQDPALLDELD 301
Cdd:pfam02463  229 LDYLKLNEERIDLLQELLRDEQEEieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQE--EELKLLAKEEEELKSELLKLE 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   302 NRISKTIQLARKHHITNETLWQHHQKLQQ---ELQTLLDFEDD----EEQLIAEEQQAHQKCIQLAEQIYQKRCEAGQKL 374
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEKEeieELEKELKELEIkreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
                          410
                   ....*....|....*
gi 572168737   375 AEQVTQQIKQLAMEN 389
Cdd:pfam02463  387 SSAAKLKEEELELKS 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
155-388 5.34e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 155 LLDEMAEQYqiwRKLHKQV------KNFRQQCQENEARKQLLQYQV--EELDEFAIKEGEFE-QLEEDQARLANAEQLLD 225
Cdd:COG1196  194 ILGELERQL---EPLERQAekaeryRELKEELKELEAELLLLKLREleAELEELEAELEELEaELEELEAELAELEAELE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 226 VSQSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHyssALDMLNEALIQIQEASSEISQLAGNIEQDPALLDELDNRIs 305
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEEL- 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 306 ktiqlarkhhitnETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCIQLAEQIyQKRCEAGQKLAEQVTQQIKQL 385
Cdd:COG1196  347 -------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEAL 412

                 ...
gi 572168737 386 AME 388
Cdd:COG1196  413 LER 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
14-388 1.25e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    14 VLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESS--------MIRNG------VDKADITATFSmqtdspaflwlKE 79
Cdd:TIGR02168   18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKAlrggkmedVIFNGsetrkpLSLAEVELVFD-----------NS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737    80 HELLDSDNPNECILRRMITIEGRSKAFVNNHPLPISQLREL--------------GQYLIHLNGQHAPQLLL-------- 137
Cdd:TIGR02168   87 DGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLfldtglgkrsysiiEQGKISEIIEAKPEERRaifeeaag 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   138 ---------KSEYQLELVN-NYADLHSLLDEMAEQyqiWRKLHKQVK---NFRQ-QCQENEARKQLLQYQVEELDE---- 199
Cdd:TIGR02168  167 iskykerrkETERKLERTReNLDRLEDILNELERQ---LKSLERQAEkaeRYKElKAELRELELALLVLRLEELREelee 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   200 --FAIKEGEfEQLEEDQARLANAEQLLDVSQSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQ 277
Cdd:TIGR02168  244 lqEELKEAE-EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   278 EASSEISQLAGNIEQDPALLDELDNRISKTIQLARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQAHQKCI 357
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          410       420       430
                   ....*....|....*....|....*....|.
gi 572168737   358 QLAEqiyqKRCEAGQKLAEQVTQQIKQLAME 388
Cdd:TIGR02168  403 ERLE----ARLERLEDRRERLQQEIEELLKK 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
150-352 1.92e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 150 ADLHSLLDEMAEQYQIWRKLHKQVKNFRQQCQENEARKQLLQYQVEEL-DEFAIKEGEFEQLEEDQARL-ANAEQLLDVS 227
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeQELAALEAELAELEKEIAELrAELEAQKEEL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737 228 QSVMGALSDNDLNIDTMLYRAIRDLEELVEMDSHYSSALDMLNEALIQIQEASSEISQLAGNIEQDPA----LLDELDNR 303
Cdd:COG4942  107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAeleaLLAELEEE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 572168737 304 ISKTIQLARKHHITNETLWQHHQKLQQELQTLLDFEDDEEQLIAEEQQA 352
Cdd:COG4942  187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-66 2.06e-03

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 39.22  E-value: 2.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572168737   1 HLTINHF-AIVRHLVLELNEGMSVITGETGAGKSIGIDALGLCLGYRSESS------MIRNGVDKADITATFS 66
Cdd:COG0419    4 RLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRsklrsdLINVGSEEASVELEFE 76
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
144-335 3.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  144 ELVNNYADL---HSLLDEMAEQyqiwRKLHKQVKNFRQQCQENEARKQLLQYQVEELD------EFAIKEGEFEQLEEDQ 214
Cdd:COG4913   229 ALVEHFDDLeraHEALEDAREQ----IELLEPIRELAERYAAARERLAELEYLRAALRlwfaqrRLELLEAELEELRAEL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737  215 ARLANAEQLLDVSQ--------SVMGALSDNDLNIDTMLYRAIRDLEELVEmdsHYSSALDMLNEALIQIQ-EASSEISQ 285
Cdd:COG4913   305 ARLEAELERLEARLdalreeldELEAQIRGNGGDRLEQLEREIERLERELE---ERERRRARLEALLAALGlPLPASAEE 381
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 572168737  286 LAGNIEQDPALLDELDNRISKTIQLARKHHITNETLWQHHQKLQQELQTL 335
Cdd:COG4913   382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1-68 4.85e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 37.72  E-value: 4.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572168737   1 HLTINHFAIVR-HLVLELNEG-MSVITGETGAGKSIGIDALGLCLGYRSESSMIRNGVDKADITATFSMQ 68
Cdd:cd03227    1 KIVLGRFPSYFvPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAE 70
 
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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