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Conserved domains on  [gi|446803709|ref|WP_000880965|]
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MULTISPECIES: DNA repair protein RecN [Salmonella]

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

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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: 1112.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  81 EENQLEEGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQMA 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 161 ARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLADGEDV 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 241 NLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 321 ALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 401 EHHLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446803709 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKELLAA 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: 1112.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  81 EENQLEEGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQMA 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 161 ARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLADGEDV 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 241 NLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 321 ALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 401 EHHLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446803709 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKELLAA 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: 746.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWL 80
Cdd:COG0497    1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  81 EENQLE-EGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQM 159
Cdd:COG0497   81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 160 AARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLaDGED 239
Cdd:COG0497  161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-SGGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 240 VNLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKHHVSP 319
Cdd:COG0497  240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 320 EALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTIDVKF 399
Cdd:COG0497  320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 400 DEHhLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
Cdd:COG0497  400 LEE-PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446803709 480 LGESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKELLAA 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 1.38e-164

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: 479.61  E-value: 1.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTP-AALRW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDdADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   80 LEENQLEE---GRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALA 156
Cdd:TIGR00634  81 LQAIELEEedeDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  157 QQMAARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLAD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  237 GEDVNLQSQLYSAKQLVSELVG-MDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  316 HVSPEALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  396 DVKFDE-----HHLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTA 470
Cdd:TIGR00634 401 EIKTSLpsgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  471 AVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKEL 550
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  ...
gi 446803709  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 3.90e-66

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: 215.91  E-value: 3.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWLE 81
Cdd:cd03241    1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446803709  82 ENQLEEGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDS 148
Cdd:cd03241   81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
AAA_23 pfam13476
AAA domain;
5-199 3.78e-15

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 74.07  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    5 LTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALK-DTPAALRWLEEN 83
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEgKGKAYVEITFEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   84 QLEEGRECLLRR--VISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDsyanEAALAQQMAA 161
Cdd:pfam13476  81 NDGRYTYAIERSreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFE----RKEKKERLEE 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 446803709  162 RYQLwhqscRDLAHHQQQSQERAARAELLQYQLKELND 199
Cdd:pfam13476 157 LEKA-----LEEKEDEKKLLEKLLQLKEKKKELEELKE 189
 
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: 1112.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWL 80
Cdd:PRK10869   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  81 EENQLEEGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQMA 160
Cdd:PRK10869  81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 161 ARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLADGEDV 240
Cdd:PRK10869 161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 241 NLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKHHVSPE 320
Cdd:PRK10869 241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 321 ALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTIDVKFD 400
Cdd:PRK10869 321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 401 EHHLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
Cdd:PRK10869 401 PEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQL 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446803709 481 GESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKELLAA 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: 746.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWL 80
Cdd:COG0497    1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  81 EENQLE-EGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQM 159
Cdd:COG0497   81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 160 AARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLaDGED 239
Cdd:COG0497  161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEAL-SGGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 240 VNLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKHHVSP 319
Cdd:COG0497  240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 320 EALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTIDVKF 399
Cdd:COG0497  320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 400 DEHhLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
Cdd:COG0497  400 LEE-PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446803709 480 LGESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKELLAA 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 1.38e-164

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: 479.61  E-value: 1.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTP-AALRW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDdADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   80 LEENQLEE---GRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALA 156
Cdd:TIGR00634  81 LQAIELEEedeDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  157 QQMAARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLAD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  237 GEDVNLQSQLYSAKQLVSELVG-MDSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAKQISLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEAQLALASvIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  316 HVSPEALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQQALETAQALHQQRQFYAQELGQLITESMHLLSMPHGLFTI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  396 DVKFDE-----HHLSNDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTA 470
Cdd:TIGR00634 401 EIKTSLpsgakARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  471 AVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGGSEVTRNTLANAKEL 550
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  ...
gi 446803709  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 3.90e-66

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: 215.91  E-value: 3.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALKDTPAALRWLE 81
Cdd:cd03241    1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446803709  82 ENQLEEGRECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDS 148
Cdd:cd03241   81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
400-536 3.10e-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: 208.60  E-value: 3.10e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 400 DEHHLS--NDGADRVEFKVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLL 477
Cdd:cd03241  138 PERQLDllDGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKL 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446803709 478 RQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGAMTETHMQPLDKRARLQELARLLGG 536
Cdd:cd03241  218 KELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
AAA_23 pfam13476
AAA domain;
5-199 3.78e-15

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 74.07  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    5 LTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATRADLCARFALK-DTPAALRWLEEN 83
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEgKGKAYVEITFEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   84 QLEEGRECLLRR--VISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDsyanEAALAQQMAA 161
Cdd:pfam13476  81 NDGRYTYAIERSreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFE----RKEKKERLEE 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 446803709  162 RYQLwhqscRDLAHHQQQSQERAARAELLQYQLKELND 199
Cdd:pfam13476 157 LEKA-----LEEKEDEKKLLEKLLQLKEKKKELEELKE 189
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-90 1.43e-08

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 55.02  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNF-AIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEA------DMVRTGATRADLCARFALKDT 73
Cdd:COG0419    1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSrsklrsDLINVGSEEASVELEFEHGGK 80
                         90
                 ....*....|....*..
gi 446803709  74 PAALRWLEENQLEEGRE 90
Cdd:COG0419   81 RYRIERRQGEFAEFLEA 97
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
431-496 7.69e-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: 7.69e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446803709 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 2.33e-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: 53.08  E-value: 2.33e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGR 49
Cdd:COG3593    3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
2-64 7.02e-07

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: 49.90  E-value: 7.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEA--------DMVRTGATRADL 64
Cdd:cd03276    1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDtnrgsslkDLIKDGESSAKI 71
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
5-98 1.01e-06

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: 49.53  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   5 LTISNFAIVRE-LEIDFQSGMTVITGETGAGKSIAIDALGLCL---------GGRAEADMVRTGATRADLCARFalkdtp 74
Cdd:cd03240    4 LSIRNIRSFHErSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtgelppnskGGAHDPKLIREGEVRAQVKLAF------ 77
                         90       100
                 ....*....|....*....|....
gi 446803709  75 aalrwleenQLEEGRECLLRRVIS 98
Cdd:cd03240   78 ---------ENANGKKYTITRSLA 92
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1-381 1.09e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709     1 MLAQLTISNF-AIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGG------RAE--ADMVRTG----ATRADLCAR 67
Cdd:pfam02463    1 YLKRIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErsakslRSErlSDLIHSKsgafVNSAEVEIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    68 FalkDTPAALRWLEENQLEegreclLRRVISSDGRSRGFINGTAVPLSQLRELGQLL--------IQIHGQHAHQQLTKP 139
Cdd:pfam02463   81 F---DNEDHELPIDKEEVS------IRRRVYRGGDSEYYINGKNVTKKEVAELLESQgispeaynFLVQGGKIEIIAMMK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   140 EQQKSLLDSYANEAALAQQMAARYqlwhqscRDLAHHQQQSQERAARAELLQYQLKELNDFNPQAGEFEQIDEEyKRLAN 219
Cdd:pfam02463  152 PERRLEIEEEAAGSRLKRKKKEAL-------KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK-LELEE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   220 SGQLLTTSQNALA--------LLADGEDVNLQSQLYSAK-----QLVSELVGMDSKLSGILDMLEEATI-QLTEASDELR 285
Cdd:pfam02463  224 EYLLYLDYLKLNEeridllqeLLRDEQEEIESSKQEIEKeeeklAQVLKENKEEEKEKKLQEEELKLLAkEEEELKSELL 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   286 HYCERLDLDPNRLFELEQRIAKQISLARKHHVSPEALPQLYQSLLEEQQQLDDQADSLETLTLAvNKHHQQALETAQALH 365
Cdd:pfam02463  304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK-LEQLEEELLAKKKLE 382
                          410
                   ....*....|....*.
gi 446803709   366 QQRQFYAQELGQLITE 381
Cdd:pfam02463  383 SERLSSAAKLKEEELE 398
recF PRK00064
recombination protein F; Reviewed
2-124 1.36e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 50.54  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGR-----AEADMVRTGATRADLCARFAlkdtpaa 76
Cdd:PRK00064   3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRshrtaRDKELIRFGAEAAVIHGRVE------- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446803709  77 lrwleenqlEEGRECLLRRVISSDGRSRGFINGTavPLSQLRELGQLL 124
Cdd:PRK00064  76 ---------KGGRELPLGLEIDKKGGRKVRINGE--PQRKLAELAGLL 112
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
2-123 4.52e-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: 48.45  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGR-----AEADMVRTGATRADLCARFalkdtpaa 76
Cdd:cd03242    1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKshrtsRDKELIRWGAEEAKISAVL-------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446803709  77 lrwleENQleeGRECLLRRVISSDGRSRGFINGTAVPlSQLRELGQL 123
Cdd:cd03242   73 -----ERQ---GGELALELTIRSGGGRKARLNGIKVR-RLSDLLGVL 110
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
432-496 2.95e-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: 44.54  E-value: 2.95e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446803709 432 SGGELSRIALAIQVITARKMetpaLIFDEVDVGISGPTAAVVGKLLRQLGES-TQVMCVTHLPQVA 496
Cdd:cd00267   82 SGGQRQRVALARALLLNPDL----LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELA 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-381 4.30e-05

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: 46.59  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709     2 LAQLTISNF-AIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLG--------GRAEADMV------RTGATRADLCA 66
Cdd:TIGR02168    2 LKKLELAGFkSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeqsakalrGGKMEDVIfngsetRKPLSLAEVEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    67 RFALKDTPAALRWLEENQleegreclLRRVISSDGRSRGFINGTAVPLSQLREL------GQLLIQIHGQHAHQQLT--K 138
Cdd:TIGR02168   82 VFDNSDGLLPGADYSEIS--------ITRRLYRDGESEYFINGQPCRLKDIQDLfldtglGKRSYSIIEQGKISEIIeaK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   139 PEQQKSLLDsyanEAA-----------------LAQQMAARYQ------------LWHQSCRDLAHHQQQSQERAARAEL 189
Cdd:TIGR02168  154 PEERRAIFE----EAAgiskykerrketerkleRTRENLDRLEdilnelerqlksLERQAEKAERYKELKAELRELELAL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   190 LQYQLKELND----FNPQAGEFEQIDEEYKR-LANSGQLLTTSQnaLALLADGEDVN-LQSQLYSAKQLVSELVGM---- 259
Cdd:TIGR02168  230 LVLRLEELREeleeLQEELKEAEEELEELTAeLQELEEKLEELR--LEVSELEEEIEeLQKELYALANEISRLEQQkqil 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   260 DSKLSGILDMLEEATIQLTEASDELRHYCERLDLDPNRLFELEQRIAkqiSLARKHHVSPEALPQLYQSLLEEQQQLDDQ 339
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE---SLEAELEELEAELEELESRLEELEEQLETL 384
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 446803709   340 ADSLETLTLAV---NKHHQQALETAQALHQQRQFYAQELGQLITE 381
Cdd:TIGR02168  385 RSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELLKK 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
116-369 8.58e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 116 QLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQMAARYQlwhqscrDLAHHQQQSQERAARAELLQYQLK 195
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEAEEELEEAEAELA 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 196 ELNDfnpqagefEQIDEEYKRLANSGQLLTTSQNALALLAdgEDVNLQSQLYSAKQLVSELVGMDSKLSGILDMLEEATI 275
Cdd:COG1196  362 EAEE--------ALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 276 QLTEASDELRHycERLDLDpnrlfELEQRIAKQISLARKHHVSPEALPQLYQSLLEEQQQLDDQADSLETLTLAVNKHHQ 355
Cdd:COG1196  432 ELEEEEEEEEE--ALEEAA-----EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
                        250
                 ....*....|....
gi 446803709 356 QALETAQALHQQRQ 369
Cdd:COG1196  505 GFLEGVKAALLLAG 518
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
2-47 1.16e-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: 43.22  E-value: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446803709   2 LAQLTISNF-AIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLG 47
Cdd:cd03278    1 LKKLELKGFkSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLG 47
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
420-491 1.28e-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: 43.22  E-value: 1.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446803709 420 PGQPLQPIAkVASGGELSRIALAiqVITARKMETPA--LIFDEVDVGISGPTAAVVGKLLRQLGESTQVMCVTH 491
Cdd:cd03278  104 PGKKVQRLS-LLSGGEKALTALA--LLFAIFRVRPSpfCVLDEVDAALDDANVERFARLLKEFSKETQFIVITH 174
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
4-61 1.52e-04

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: 42.35  E-value: 1.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   4 QLTISNFAIVR-ELEIDFQSG-MTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGATR 61
Cdd:cd03227    1 KIVLGRFPSYFvPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKA 60
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
4-53 2.95e-04

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: 42.26  E-value: 2.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446803709   4 QLTISNF-AIVRELEIDFQ----SGMTVITGETGAGKSIAIDALGLCLGGRAEAD 53
Cdd:cd03279    5 KLELKNFgPFREEQVIDFTgldnNGLFLICGPTGAGKSTILDAITYALYGKTPRY 59
mukB PRK04863
chromosome partition protein MukB;
177-377 4.21e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  177 QQQSQERAARAEL--LQYQLKELNDFNPQAGE--------FEQIDEEYKRLANSgqlLTTSQNALALLadgEDVNLQSQ- 245
Cdd:PRK04863  345 RQQEKIERYQADLeeLEERLEEQNEVVEEADEqqeenearAEAAEEEVDELKSQ---LADYQQALDVQ---QTRAIQYQq 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  246 ----LYSAKQLvseLVGMDSKLSGILDMLEEATIQLTEASDELRHYCERLDL--DPNRLFE----LEQRIAKQISLARKH 315
Cdd:PRK04863  419 avqaLERAKQL---CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVaqAAHSQFEqayqLVRKIAGEVSRSEAW 495
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446803709  316 HVSPEALPQlyqslLEEQQQLDDQADSLEtltlavNKHH--QQALETAQALHQQRQFYAQELGQ 377
Cdd:PRK04863  496 DVARELLRR-----LREQRHLAEQLQQLR------MRLSelEQRLRQQQRAERLLAEFCKRLGK 548
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
412-491 4.59e-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: 43.13  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   412 VEFKVTTNpGQPLQPIAKVaSGGELSRIALAIqvITARKMETPALI--FDEVDVGISGPTAAVVGKLLRQLGESTQVMCV 489
Cdd:TIGR02169 1058 LELSAKPK-GKPVQRLEAM-SGGEKSLTALSF--IFAIQRYKPSPFyaFDEVDMFLDGVNVERVAKLIREKAGEAQFIVV 1133

                   ..
gi 446803709   490 TH 491
Cdd:TIGR02169 1134 SL 1135
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-78 6.40e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 42.23  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   1 MLAQLTISNFAIVRELEIDFqSGMTVITGETGAGKSIAIDALGL---CLGGRAEADMVRTGATRADLCARFALKDTPAAL 77
Cdd:COG4637    1 MITRIRIKNFKSLRDLELPL-GPLTVLIGANGSGKSNLLDALRFlsdAARGGLQDALARRGGLEELLWRGPRTITEPIRL 79

                 .
gi 446803709  78 R 78
Cdd:COG4637   80 E 80
PRK01156 PRK01156
chromosome segregation protein; Provisional
1-59 6.62e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 6.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446803709   1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGG----RAEADMVRTGA 59
Cdd:PRK01156   2 IIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTdkrtEKIEDMIKKGK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-380 1.40e-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: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   115 SQLRELGQLLIQIHGQHAHQQLTKPEQQKSLLDSYANEAALAQQMAARYQLWHQSCRDLAHHQQQSQERAARAELLQYQL 194
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   195 KELND-FNPQAGEFEQIDEEYKRLANSGQLLTTSQNALALLADGEDVNLQSQLYSAKQLVSELVGMDSKLSGILDMLEEA 273
Cdd:TIGR02168  340 AELEEkLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   274 TIQLTEASDEL-----RHYCERLDLDPNRLFELEQRIAKQISLARKHHVSPEALPQLYQSLLEEQQQLDDQADSLETLTL 348
Cdd:TIGR02168  420 QQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
                          250       260       270
                   ....*....|....*....|....*....|....
gi 446803709   349 AVNKHHQQAletAQALHQQRQF--YAQELGQLIT 380
Cdd:TIGR02168  500 NLEGFSEGV---KALLKNQSGLsgILGVLSELIS 530
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
17-120 1.42e-03

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: 41.59  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709    17 EIDFQSGMTVITGETGAGKSIAIDALGLCLGG------RAE--ADMVRTG-----ATRADLCARFALKDTPAALRWleen 83
Cdd:TIGR02169   18 VIPFSKGFTVISGPNGSGKSNIGDAILFALGLssskamRAErlSDLISNGkngqsGNEAYVTVTFKNDDGKFPDEL---- 93
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 446803709    84 qleegrECLLRRVISSDGR-SRGFINGTAVPLSQLREL 120
Cdd:TIGR02169   94 ------EVVRRLKVTDDGKySYYYLNGQRVRLSEIHDF 125
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-373 3.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709   2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKS--------IAIDALglclggRAEADMVRTGATRADLCARFALKDT 73
Cdd:COG4717    3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKStllafiraMLLERL------EKEADELFKPQGRKPELNLKELKEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709  74 PAALRWLEEnQLEEGRECLLRRVISSdgrsrgfingtavplSQLRELGQLLiqihgQHAHQQLTKPEQQKSLLDSYANEA 153
Cdd:COG4717   77 EEELKEAEE-KEEEYAELQEELEELE---------------EELEELEAEL-----EELREELEKLEKLLQLLPLYQELE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 154 ALAQQMA---ARYQLWHQSCRDLAHHQQQSQERAARAELLQYQLKELNDFNPQA--GEFEQIDEEYKRL----ANSGQLL 224
Cdd:COG4717  136 ALEAELAelpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELqqrlAELEEEL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 225 TTSQNALA--------LLADGEDVNLQSQLYSAKQL------VSELVGMDSKLSGILDMLEEATIQLTEASDELRHYCER 290
Cdd:COG4717  216 EEAQEELEeleeeleqLENELEAAALEERLKEARLLlliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803709 291 LDLDPNRLFELEQRIAKQISLAR--------KHHVSPEALPQLYQSLLEEQQQLDDQADSLETLtlavnkhhQQALETAQ 362
Cdd:COG4717  296 EKASLGKEAEELQALPALEELEEeeleellaALGLPPDLSPEELLELLDRIEELQELLREAEEL--------EEELQLEE 367
                        410
                 ....*....|.
gi 446803709 363 ALHQQRQFYAQ 373
Cdd:COG4717  368 LEQEIAALLAE 378
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
2-42 3.31e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 39.89  E-value: 3.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446803709    2 LAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDAL 42
Cdd:pfam13175   3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
AAA_29 pfam13555
P-loop containing region of AAA domain;
22-42 8.15e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 34.88  E-value: 8.15e-03
                          10        20
                  ....*....|....*....|.
gi 446803709   22 SGMTVITGETGAGKSIAIDAL 42
Cdd:pfam13555  22 RGNTLLTGPSGSGKSTLLDAI 42
 
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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