NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|693211162|ref|WP_032329998|]
View 

DNA repair protein RecN [Escherichia coli]

Protein Classification

DNA repair protein RecN( domain architecture ID 11485034)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-553 0e+00

recombination and repair protein; Provisional


:

Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 1115.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  81 EENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQLQEMT 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 161 ARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDA 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 241 NLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 321 ALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 401 EHHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 693211162 481 GESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
Cdd:PRK10869 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-553 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 1115.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  81 EENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQLQEMT 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 161 ARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDA 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 241 NLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 321 ALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 401 EHHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 693211162 481 GESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
Cdd:PRK10869 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-553 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 754.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWL 80
Cdd:COG0497    1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  81 EENQLE-DGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQLQEM 159
Cdd:COG0497   81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 160 TARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMaDGED 239
Cdd:COG0497  161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-SGGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 240 ANLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSP 319
Cdd:COG0497  240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 320 EALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTIDVKF 399
Cdd:COG0497  320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 400 DEHhLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
Cdd:COG0497  400 LEE-PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693211162 480 LGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
Cdd:COG0497  479 LARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLAL 552
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-553 1.86e-173

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: 501.96  E-value: 1.86e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTP-AALCW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDdADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   80 LEENQLED---GHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQL 156
Cdd:TIGR00634  81 LQAIELEEedeDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  157 QEMTARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMAD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  237 GEDANLQSQLYTAKQLVSELIG-MDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  316 HVSPEALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  396 DVKFDE-----HHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTA 470
Cdd:TIGR00634 401 EIKTSLpsgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  471 AVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKEL 550
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  ...
gi 693211162  551 LAA 553
Cdd:TIGR00634 561 LEA 563
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-148 3.36e-68

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: 221.31  E-value: 3.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWLE 81
Cdd:cd03241    1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 693211162  82 ENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDG 148
Cdd:cd03241   81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
AAA_23 pfam13476
AAA domain;
5-182 1.83e-14

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 72.14  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    5 LTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWLEENQ 84
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   85 LEDGHECLLRR---VISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPE---------HQKFLLDGYANE 152
Cdd:pfam13476  81 NDGRYTYAIERsreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQereeeferkEKKERLEELEKA 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 693211162  153 TSQLQEMTARYQLWHQSCRDLAHHQQLSQE 182
Cdd:pfam13476 161 LEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-553 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 1115.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  81 EENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQLQEMT 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 161 ARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDA 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 241 NLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 321 ALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 401 EHHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 693211162 481 GESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
Cdd:PRK10869 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-553 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 754.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWL 80
Cdd:COG0497    1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  81 EENQLE-DGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQLQEM 159
Cdd:COG0497   81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 160 TARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMaDGED 239
Cdd:COG0497  161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-SGGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 240 ANLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSP 319
Cdd:COG0497  240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 320 EALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTIDVKF 399
Cdd:COG0497  320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 400 DEHhLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
Cdd:COG0497  400 LEE-PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693211162 480 LGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
Cdd:COG0497  479 LARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLAL 552
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-553 1.86e-173

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: 501.96  E-value: 1.86e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTP-AALCW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDdADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   80 LEENQLED---GHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSQL 156
Cdd:TIGR00634  81 LQAIELEEedeDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  157 QEMTARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMAD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  237 GEDANLQSQLYTAKQLVSELIG-MDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  316 HVSPEALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQALETARALHQQRQHYANELAQLITDSMHALSMPHGQFTI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  396 DVKFDE-----HHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTA 470
Cdd:TIGR00634 401 EIKTSLpsgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  471 AVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGGSEVTRNTLANAKEL 550
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  ...
gi 693211162  551 LAA 553
Cdd:TIGR00634 561 LEA 563
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-148 3.36e-68

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: 221.31  E-value: 3.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWLE 81
Cdd:cd03241    1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 693211162  82 ENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDG 148
Cdd:cd03241   81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
390-536 1.48e-63

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: 209.37  E-value: 1.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 390 HGQ-FTIDVKFDEHHLGA--DGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGIS 466
Cdd:cd03241  127 HGQhDHQNLLNPERQLDLldGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGIS 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 467 GPTAAVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLDKKARLQELARLLGG 536
Cdd:cd03241  207 GEVAQAVGKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
AAA_23 pfam13476
AAA domain;
5-182 1.83e-14

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 72.14  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    5 LTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALCWLEENQ 84
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   85 LEDGHECLLRR---VISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPE---------HQKFLLDGYANE 152
Cdd:pfam13476  81 NDGRYTYAIERsreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQereeeferkEKKERLEELEKA 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 693211162  153 TSQLQEMTARYQLWHQSCRDLAHHQQLSQE 182
Cdd:pfam13476 161 LEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-73 4.40e-09

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 56.56  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNF-AIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEA------DMVRTGAARADLCARFSLKDT 73
Cdd:COG0419    1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSrsklrsDLINVGSEEASVELEFEHGGK 80
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1-388 1.83e-08

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: 57.29  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162     1 MLAQLTISNF-AIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGG------RAE--ADMVRTGAARADLCARFSL- 70
Cdd:pfam02463    1 YLKRIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErsakslRSErlSDLIHSKSGAFVNSAEVEIt 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    71 -KDTPAALcwleenqLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLREL---------------GQLLIQIhgqhahQ 134
Cdd:pfam02463   81 fDNEDHEL-------PIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELlesqgispeaynflvQGGKIEI------I 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   135 LLTKPEHQKFLLDG------YANETSQLQEM--TARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQpgE 206
Cdd:pfam02463  148 AMMKPERRLEIEEEaagsrlKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--Y 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   207 FEQIDEEY---KRLANSGQLLTTSQNALALMADGEDANLQSQlytakQLVSELIGMDSKLSGVLDMLEEATI-QIAEASD 282
Cdd:pfam02463  226 LLYLDYLKlneERIDLLQELLRDEQEEIESSKQEIEKEEEKL-----AQVLKENKEEEKEKKLQEEELKLLAkEEEELKS 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   283 ELRHYCDRLDLDPNRLFELEQRISK--------QISLARKHHVSPEALPQYYQSLLEEQQQLDNQADSQETLALAVTKH- 353
Cdd:pfam02463  301 ELLKLERRKVDDEEKLKESEKEKKKaekelkkeKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKk 380
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 693211162   354 -HQQALETARALHQQRQHYANELAQLITDSMHALSM 388
Cdd:pfam02463  381 lESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
431-496 7.47e-08

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: 51.98  E-value: 7.47e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 693211162 431 ASGGELSRIALAIQVITARKMETPALIFDEVDVGISG-PTAAVVGKLLRQLGESTQVMCVTHLPQVA 496
Cdd:cd03227   78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPrDGQALAEAILEHLVKGAQVIVITHLPELA 144
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-49 2.85e-07

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: 52.70  E-value: 2.85e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGR 49
Cdd:COG3593    3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
recF PRK00064
recombination protein F; Reviewed
2-124 3.88e-07

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 52.47  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGR-----AEADMVRTGAARADLCARFSlkdtpaa 76
Cdd:PRK00064   3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRshrtaRDKELIRFGAEAAVIHGRVE------- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 693211162  77 lcwleenqlEDGHECLLRRVISSDGRSRGFINGTavPLSQLRELGQLL 124
Cdd:PRK00064  76 ---------KGGRELPLGLEIDKKGGRKVRINGE--PQRKLAELAGLL 112
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
5-70 5.24e-07

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: 50.30  E-value: 5.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 693211162   5 LTISNFAIVRE-LEIDFHSGMTVITGETGAGKSIAIDALGLCL---------GGRAEADMVRTGAARADLCARFSL 70
Cdd:cd03240    4 LSIRNIRSFHErSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtgelppnskGGAHDPKLIREGEVRAQVKLAFEN 79
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
2-123 1.25e-06

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: 49.99  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGR-----AEADMVRTGAARADLCARFSlkdtpaa 76
Cdd:cd03242    1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKshrtsRDKELIRWGAEEAKISAVLE------- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 693211162  77 lcwleenqlEDGHECLLRRVISSDGRSRGFINGTAVPlSQLRELGQL 123
Cdd:cd03242   74 ---------RQGGELALELTIRSGGGRKARLNGIKVR-RLSDLLGVL 110
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
2-64 3.89e-06

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: 47.59  E-value: 3.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEA--------DMVRTGAARADL 64
Cdd:cd03276    1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDtnrgsslkDLIKDGESSAKI 71
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
4-70 8.75e-06

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: 46.20  E-value: 8.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693211162   4 QLTISNFAIVR-ELEIDFHSG-MTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSL 70
Cdd:cd03227    1 KIVLGRFPSYFvPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSA 69
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
432-496 2.14e-05

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 44.93  E-value: 2.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 693211162 432 SGGELSRIALAIQVITARKMetpaLIFDEVDVGISGPTAAVVGKLLRQLGES-TQVMCVTHLPQVA 496
Cdd:cd00267   82 SGGQRQRVALARALLLNPDL----LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELA 143
PRK01156 PRK01156
chromosome segregation protein; Provisional
1-378 2.54e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGG----RAEADMVRTGAARADLCARFSLkdtpaa 76
Cdd:PRK01156   2 IIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTdkrtEKIEDMIKKGKNNLEVELEFRI------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  77 lcwleenqleDGHECLLRRVISSDGR---------------SRGF------INGTAVPLSQLRELGQLLIQiHGQHAHQL 135
Cdd:PRK01156  76 ----------GGHVYQIRRSIERRGKgsrreayikkdgsiiAEGFddttkyIEKNILGISKDVFLNSIFVG-QGEMDSLI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 136 LTKPEHQKFLLDgyanETSQLQEMTARYQLWHQSCRDLahHQQLSQERAARAELLQYQLkELNEFNPQPGEFEQ----ID 211
Cdd:PRK01156 145 SGDPAQRKKILD----EILEINSLERNYDKLKDVIDML--RAEISNIDYLEEKLKSSNL-ELENIKKQIADDEKshsiTL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 212 EEYKRLANSGQLLTTSQNalalMADGEDANLQSQLYTAKQLVSELIGMDSKLSgvldMLEEATIQIAEASDEL------- 284
Cdd:PRK01156 218 KEIERLSIEYNNAMDDYN----NLKSALNELSSLEDMKNRYESEIKTAESDLS----MELEKNNYYKELEERHmkiindp 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 285 ----RHYCDRLDLDPNRLFELEQRISK---QISLARKHHVSPEALPQYYQSLLEEQQQ---LDNQADSQETLALavtkHH 354
Cdd:PRK01156 290 vyknRNYINDYFKYKNDIENKKQILSNidaEINKYHAIIKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEM----DY 365
                        410       420
                 ....*....|....*....|....
gi 693211162 355 QQALETARALHQQRQHYANELAQL 378
Cdd:PRK01156 366 NSYLKSIESLKKKIEEYSKNIERM 389
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
4-70 6.35e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 44.18  E-value: 6.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 693211162   4 QLTISNF-AIVRELEIDF----HSGMTVITGETGAGKSIAIDALGLCLGGRAEAD----MVRTGAARADLCARFSL 70
Cdd:cd03279    5 KLELKNFgPFREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYgrqeNLRSVFAPGEDTAEVSF 80
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
415-491 7.12e-05

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 43.99  E-value: 7.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693211162 415 RVTTNPGQPMQPIAkVASGGELSRIALAiqVITARKMETPA--LIFDEVDVGISGPTAAVVGKLLRQLGESTQVMCVTH 491
Cdd:cd03278   99 EIIEAPGKKVQRLS-LLSGGEKALTALA--LLFAIFRVRPSpfCVLDEVDAALDDANVERFARLLKEFSKETQFIVITH 174
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
2-47 1.70e-04

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 42.84  E-value: 1.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 693211162   2 LAQLTISNF-AIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLG 47
Cdd:cd03278    1 LKKLELKGFkSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLG 47
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-378 2.63e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELEIDFHSGMTVITGETGAGKS--------IAIDALglclggRAEADMVRTGAARADLCARFSLKDT 73
Cdd:COG4717    3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKStllafiraMLLERL------EKEADELFKPQGRKPELNLKELKEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162  74 PAALCWLEENqlEDGHECLLRRVISSDGRsrgfINGTAVPLSQLR-ELGQLLIQIHGQHAHQLLTKPEHQkflldgYANE 152
Cdd:COG4717   77 EEELKEAEEK--EEEYAELQEELEELEEE----LEELEAELEELReELEKLEKLLQLLPLYQELEALEAE------LAEL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 153 TSQLQEMTARYQLWHQSCRDLAH-HQQLSQERAARAELLQY-QLKELNEFNPQPGEFEQIDEEYKRL-----ANSGQLLT 225
Cdd:COG4717  145 PERLEELEERLEELRELEEELEElEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELeeeleEAQEELEE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 226 TSQNALALMADGEDANLQSQLYTAKQL------VSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLF 299
Cdd:COG4717  225 LEEELEQLENELEAAALEERLKEARLLlliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162 300 ELEQRISKQISLAR------------KHHVSPEALPQYYQSLLEEQQQLDNQADSQETLALAVTKHHQQAL--------- 358
Cdd:COG4717  305 EELQALPALEELEEeeleellaalglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagvede 384
                        410       420
                 ....*....|....*....|
gi 693211162 359 ETARALHQQRQHYANELAQL 378
Cdd:COG4717  385 EELRAALEQAEEYQELKEEL 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
17-120 2.77e-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: 43.90  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    17 EIDFHSGMTVITGETGAGKSIAIDALGLCLGG------RAE--ADMVRTG--AARADLCA---RFSlkdtpaalcwLEEN 83
Cdd:TIGR02169   18 VIPFSKGFTVISGPNGSGKSNIGDAILFALGLssskamRAErlSDLISNGknGQSGNEAYvtvTFK----------NDDG 87
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 693211162    84 QLEDGHECLLRRVISSDGR-SRGFINGTAVPLSQLREL 120
Cdd:TIGR02169   88 KFPDELEVVRRLKVTDDGKySYYYLNGQRVRLSEIHDF 125
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-77 3.56e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 43.00  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   1 MLAQLTISNFAIVRELEIDFHsGMTVITGETGAGKSIAIDALGL---CLGGRAEADMVRTGAARADLCARFSLKDTPAAL 77
Cdd:COG4637    1 MITRIRIKNFKSLRDLELPLG-PLTVLIGANGSGKSNLLDALRFlsdAARGGLQDALARRGGLEELLWRGPRTITEPIRL 79
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-378 5.94e-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: 42.74  E-value: 5.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162     2 LAQLTISNF-AIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLG--------GRAEADMV------RTGAARADLCA 66
Cdd:TIGR02168    2 LKKLELAGFkSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeqsakalrGGKMEDVIfngsetRKPLSLAEVEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162    67 RFSLKDTPAAlcwleenqLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLREL--------GQLLIQIHGQHAHQLLTK 138
Cdd:TIGR02168   82 VFDNSDGLLP--------GADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLfldtglgkRSYSIIEQGKISEIIEAK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   139 PEHQKFLLDGYA---------NET-SQLQEMTA------------RYQLWH---QSCRDLAHHQQLSQERAARAELLQYQ 193
Cdd:TIGR02168  154 PEERRAIFEEAAgiskykerrKETeRKLERTREnldrledilnelERQLKSlerQAEKAERYKELKAELRELELALLVLR 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   194 LKELNEfnpqpgEFEQIDEEYKRLAnsgQLLTTSQNALalmadgedANLQSQLYTAKQLVSEligMDSKLSGVLDMLEEA 273
Cdd:TIGR02168  234 LEELRE------ELEELQEELKEAE---EELEELTAEL--------QELEEKLEELRLEVSE---LEEEIEELQKELYAL 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   274 TIQIAEASDELRHYCDRLDLDPNRLFELEQRISKqisLARKHHVSPEALpqyyQSLLEEQQQLDNQADSQEtLALAVTKH 353
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEE---LESKLDELAEEL----AELEEKLEELKEELESLE-AELEELEA 365
                          410       420
                   ....*....|....*....|....*.
gi 693211162   354 HQQALETA-RALHQQRQHYANELAQL 378
Cdd:TIGR02168  366 ELEELESRlEELEEQLETLRSKVAQL 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
421-491 7.54e-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: 42.36  E-value: 7.54e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 693211162   421 GQPMQPIAKVaSGGELSRIALAIqvITARKMETPALI--FDEVDVGISGPTAAVVGKLLRQLGESTQVMCVTH 491
Cdd:TIGR02169 1066 GKPVQRLEAM-SGGEKSLTALSF--IFAIQRYKPSPFyaFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSL 1135
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
2-116 8.72e-04

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


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 41.02  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   2 LAQLTISNFAIVRELE-IDFHSGMTVITGETGAGKSIAIDALGLCLGgraeadmVRTGAARA----DLCARFSLKDTPAA 76
Cdd:cd03275    1 LKRLELENFKSYKGRHvIGPFDRFTCIIGPNGSGKSNLMDAISFVLG-------EKSSHLRSknlkDLIYRARVGKPDSN 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 693211162  77 LCWLEEN-QLEDGHECLLRRVISSdGRSRGFINGTAVPLSQ 116
Cdd:cd03275   74 SAYVTAVyEDDDGEEKTFRRIITG-GSSSYRINGKVVSLKE 113
COG3910 COG3910
Predicted ATPase [General function prediction only];
9-77 1.74e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 40.13  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   9 NFAIVRELE-IDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEadmvrtGAARAdlcARFSLKDTPAAL 77
Cdd:COG3910   23 NLPAVRNLEgLEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPE------GGSKN---FRFSTRESESAL 83
AAA_29 pfam13555
P-loop containing region of AAA domain;
18-42 3.04e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 36.04  E-value: 3.04e-03
                          10        20
                  ....*....|....*....|....*.
gi 693211162   18 IDFH-SGMTVITGETGAGKSIAIDAL 42
Cdd:pfam13555  17 IPIDpRGNTLLTGPSGSGKSTLLDAI 42
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-73 6.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 693211162   5 LTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDAL--------GLCLGGRAEADMVRTGAARADLCARFSLKDT 73
Cdd:PRK03918   6 LKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAIlvglywghGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
173-491 8.15e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   173 LAHHQQLSQERAARAELLQYQLKELNEFNpqpGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDANLQSQLYTAKQL 252
Cdd:pfam02463  835 LEELALELKEEQKLEKLAEEELERLEEEI---TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   253 VSELIGMDSklsgvLDMLEEATI-QIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPEALPQYYQSLLE 331
Cdd:pfam02463  912 LEEKENEIE-----ERIKEEAEIlLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEK 986
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   332 EQQQldNQADSQEtlalavtkhhqQALETARALHQQRQhyANELAQLITDSMHALSMPHGQFTIDVKFDEhhLGADGADR 411
Cdd:pfam02463  987 EERY--NKDELEK-----------ERLEEEKKKLIRAI--IEETCQRLKEFLELFVSINKGWNKVFFYLE--LGGSAELR 1049
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693211162   412 -----------IEFRVTTnPGQPMQPIaKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:pfam02463 1050 ledpddpfsggIEISARP-PGKGVKNL-DLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKEL 1127
                          330
                   ....*....|.
gi 693211162   481 GESTQVMCVTH 491
Cdd:pfam02463 1128 SKNAQFIVISL 1138
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH